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Supplier: ACROBIOSYSTEMS
Description: Cynomolgus / Rhesus macaque FcRn / FCGRT&B2M Heterodimer Protein, His Tag (BLI verified), ACROBiosystems

Supplier: Wards
Description: Did you lose something? We can help!

Catalog Number: (103010-646)
Supplier: Anaspec Inc
Description: The sequence (Accession # NP_001116849) corresponding to the full length human DJ-1 protein along with N-terminal GST tag was expressed in E. coli. The recombinant DJ-1 protein was purified from bacterial lysate using GST affinity chromatography followed by GST tag cleavage and removal. The molecular weight of the recombinant DJ-1 protein is 19.9 kDa.
DJ-1 is also known as PARK7 (Parkinson disease protein 7). It is a 189-amino acid protein that is ubiquitously expressed in many organs including brain, liver, kidney, pancreas, heart, and others. Although DJ-1 was originally discovered as a novel oncogene product, it was found to play several other roles in biological processes. This includes the regulation of RNA binding activity, fertility, anti-oxidative stress, and is linked to the early onset of Parkinson disease when mutated. Sequence (Accession# NP_001116849) corresponds to the full length human DJ-1 protein and was expressed in E. coli.


Catalog Number: (102996-158)
Supplier: Anaspec Inc
Description: This is a truncated peptide of native rat amylin. In-vivo and in-vitro studies suggest that it acts as a specific amylin antagonist. In isolated soleus muscle, it blocks amylin-induced inhibition of glycogen synthesis but has no effect in the absence of amylin. Amylin (8-37) increases whole body and muscle insulin sensitivity and consistently reduces basal insulin levels in normal and hGH-induced insulin-resistant rats. It also elicits a significant alteration of in-vivo lipid metabolism.
Sequence: ATQRLANFLVRSSNNLGPVLPPTNVGSNTY - NH2
MW: 3200.6 Da
% Peak Area by HPLC: ≥ 95%
Storage condition: -20°C


Supplier: PeproTech, Inc.
Description: Semaphorins are a large group of structurally-related, secreted, GPI-anchored, transmembrane, cell-signaling molecules. There are 8 major classifications of Semaphorins (the first seven ordered by number, 1-7, and the eighth designated V for virus), which are characterized by the existence of a conserved 500 amino acid SEMA domain at the amino terminus. Classes 3, 4, 6, and 7 are found in vertebrates only, whilst class 5 is found in both vertebrates and invertebrates. Each class is then divided into additional subgroups based on shared structural characteristics. Semaphorins primarily function as axon growth cone guidance factors during neuronal development. Semaphorin 3A acts as a chemo-repellent to axons, and an inhibitor of the growth of axons by signaling through receptors, Neuropilin-1 and Plexin-A. PeproTech's CHO cell-derived Recombinant Human Semaphorin 3A Fc is a glycosylated, disulfide-linked homodimer of 1,976 amino acid residues, which includes the SEMA domain, immunoglobulin c2-like domain, and the C-terminal basic Arg/Lys-rich domain of the mature sequence, as well as an 8-residue N-terminal His-tag and a 230-residue C-terminal Fc region linked by two glycines. Recombinant Human Semaphorin 3A Fc has a calculated molecular weight of 226.2 kDa and therefore runs above the 200kDa marker by SDS-PAGE analysis under nonreducing conditions. When run under reducing conditions, this protein migrates as three distinct bands that, due to glycosylation, run higher than expected at apparent molecular weights of approximately 120-130 kDa, 90-100 kDa, and 35-40 kDa.

Supplier: New England Biolabs (NEB)
Description: A proprietary plasmid is digested to completion with appropriate restriction enzymes to yield 11 bands suitable for use as molecular weight standards for both agarose and polyacrylamide gel electrophoresis

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Catalog Number: (76303-720)
Supplier: PeproTech, Inc.
Description: Bone morphogenetic proteins (BMPs) constitute a subfamily within the TGF-beta superfamily of structurally related signaling proteins. Members of this superfamily are widely distributed throughout the body, and are involved in diverse physiological processes during both pre- and postnatal life. Like BMP-7, BMP-4 is involved in the development and maintenance of bone and cartilage. Reduced expression of BMP-4 is associated with a number of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. Recombinant Human BMP-4, expressed in HeLa cells, is a 25.6 kDa homodimeric glycoprotein.


Supplier: VWR
Description: Bovine serum albumin, powder, Fraction V. Nuclease and protease-free. Suitable for use in most molecular biology applications.
Catalog Number: (103008-350)
Supplier: Anaspec Inc
Description: This peptide is Histone H3 amino acid residues 1-21. It is dimethylated at lysine 9 with a C-terminal GG linker followed by a biotinylated lysine. The dimethylation of Histone H3 at lysine 9 is dynamically and sex-differentially regulated during meiotic prophase. Provided at >95% peptide purity, this peptide was dissolved in distilled water at 1 mg/ml and re-lyophilized to powder form.
Sequence:ARTKQTAR-K(Me2)-STGGKAPRKQLA-GGK(Biotin)-NH2
MW:2750.2 Da
% peak area by HPLC:95
Storage condition:-20° C


Supplier: AVANTOR PERFORMANCE MATERIAL LLC
Description: For protein precipitation, liquid chromatography and molecular biology applications.
Supplier: MilliporeSigma
Catalog Number: (103010-282)
Supplier: Anaspec Inc
Description: Matrix metalloproteinases (MMPs) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components. The importance of MMPs in tumor development and invasion as well as other diseases is well known. MMP-7 (matrilysin, PUMP-1) is proposed as a potential anti-cancer drug target.

Recombinant human MMP-7 was expressed in E.coli. The molecular mass of zymogen is approximately 28-kDa on SDS-PAGE and the active form is 19-kDa.
pro-MMP-7 can be fully activated by incubating with 1 mM APMA at 37°C for 1 hr. Its activity can be measured by FRET peptides. 5-10 ng of enzyme is sufficient for FRET-based assay.


Supplier: Anaspec Inc
Description: Myelin Oligodendrocyte Glycoprotein (MOG) is a member of the immunoglobulin superfamily and is expressed exclusively in the central nervous system (CNS). Although MOG protein constitutes only 0.01-0.05% of the CNS myelin proteins, it was demonstrated that MOG protein is a crucial autoantigen for multiple sclerosis in humans and experimental autoimmune encephalomyelitis (EAE) in rodents and monkeys

The sequence (Accession #CAE84068) corresponding to the extracellular domain of rat MOG along with a 6x His tag was expressed in E. coli. The recombinant rat MOG (R-rMOG) was purified from urea denatured bacterial lysate using immobilized metal affinity chromatography (IMAC). The molecular mass of the recombinant rat MOG is 14.2 kDa.

Catalog Number: (103005-822)
Supplier: Anaspec Inc
Description: Post-mortem Alzheimer’s diseased brain specimens reveals significant levels of Aß (11-40/42) within insoluble amyloid pools. The ß-secretase enzyme or ß-amyloid precursor protein-cleaving enzyme (BACE) generates the N terminus of Aß, ultimately leading to the production of full-length Aß (1-40/42) or truncated Aß (11-40/42). The abundance of Aß (11-40/42) produced by BACE suggests that their roles in AD pathogenesis may be important.
Sequence: EVHHQKLVFFAEDVGSNKGAIIGLMVGGVV
Molecular Weight: 3151.7 Da
% Peak Area by HPLC: ≥95
Peptide Content: ≥ 60%
Storage condition: -20°C


Catalog Number: (470231-428)
Supplier: Wards
Description: Suitable for VSEPR Study


Catalog Number: (76303-722)
Supplier: PeproTech, Inc.
Description: Noggin belongs to a group of diffusible proteins that bind to ligands of the TGF-beta family, and regulate their activity by inhibiting their access to signaling receptors. The interplay between TGF-beta ligands and their natural antagonists has major biological significance during development processes, in which cellular response can vary considerably depending upon the local concentration of the signaling molecule. Noggin was originally identified as a BMP-4 antagonist whose action was critical for proper formation of the head and other dorsal structures. Consequently, noggin has been shown to modulate the activities of other BMPs including BMP-2,-7,-13, and -14. Targeted deletion of noggin in mice results in prenatal death, and a recessive phenotype displaying a severely malformed skeletal system. Conversely, transgenic mice over-expressing noggin in mature osteoblasts display impaired osteoblastic differentiation, reduced bone formation, and severe osteoporosis. Recombinant Human Noggin is a 46 kDa disulfide-linked homodimer consisting of two 205 amino acid polypeptide chains. Monomeric glycosylated noggin migrates at an apparent molecular weight of approximately 28.0-33.0 kDa by SDS PAGE analysis under reducing conditions.


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