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Name :
VAMP7 HumanDescription:
Vesicle-Associated Membrane Protein 7 Human Recombinant
Vesicle-associated membrane protein 7, Tetanus-insensitive VAMP, tetanus neurotoxin-insensitive VAMP, Synaptobrevin-like protein 1, TI-VAMP, VAMP-7, TIVAMP, SYBL1.
Product # :
PRO-1194Price :
Quantity :
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Shipped with Ice Packs
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Description
VAMP7 Human Recombinant produced in E. coli is a single polypeptide chain containing 211 amino acids (1-188) and having a molecular mass of 23.0 kDa.VAMP7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The VAMP7 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Vesicle-Associated Membrane Protein 7 (VAMP7) is a member of the synaptobrevin family. VAMP7 is a transmembrane protein, which is a member of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) family. VAMP7 is involved in the targeting and/or fusion of transport vesicles to their target membrane during transport of proteins from the early endosome to the lysosome. VAMP7 localizes to late endosomes and lysosomes and is involved in the fusion of transport vesicles to their target membranes. VAMP7 is essential for heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion. It is also necessary for calcium regulated lysosomal exocytosis. In addition, VAMP7 is involved in the export of chylomicrons from the endoplasmic reticulum to the cis Golgi. Furthermore, VAMP7 is needed for exocytosis of mediators during eosinophil and neutrophil degranulation, and target cell killing by natural killer cells.
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Synonyms
Vesicle-associated membrane protein 7, Tetanus-insensitive VAMP, tetanus neurotoxin-insensitive VAMP, Synaptobrevin-like protein 1, TI-VAMP, VAMP-7, TIVAMP, SYBL1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAILFAV VARGTTILAK HAWCGGNFLE VTEQILAKIP SENNKLTYSH GNYLFHYICQ DRIVYLCITD DDFERSRAFN FLNEIKKRFQ TTYGSRAQTA LPYAMNSEFS SVLAAQLKHH SENKGLDKVM ETQAQVDELK GIMVRNIDLV AQRGERLELL IDKTENLVDS SVTFKTTSRN LARAMCMKNL K
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MCL1 HumanDescription:
Myeloid Cell Leukemia Sequence 1 Human Recombinant
Myeloid cell leukemia sequence 1 (BCL2-related), induced myeloid leukemia cell differentiation protein Mcl-1, myeloid cell leukemia ES, Bcl-2-related protein EAT/mcl1, Bcl-2-like protein 3, MCL1-ES, MCL1S, mcl1/EAT, BCL2L3, MCL1L.
Product # :
PRO-1202Price :
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Description
MCL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 347 amino acids (1-327) and having a molecular mass of 37.2 kDa.MCL1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The MCL1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
MCL1 is a member of the Bcl-2 family. MCL1 takes part in the control of apoptosis against cell existence, and in the preservation of viability but not of proliferation. Alternative splicing happens at this locus and two transcript variants encoding different isoforms are known. Isoform 1 is the longer gene product and it increases cell existence by inhibiting apoptosis. Isoform 2 is a shorter gene product which indorses apoptosis and is death-inducing.
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Synonyms
Myeloid cell leukemia sequence 1 (BCL2-related), induced myeloid leukemia cell differentiation protein Mcl-1, myeloid cell leukemia ES, Bcl-2-related protein EAT/mcl1, Bcl-2-like protein 3, MCL1-ES, MCL1S, mcl1/EAT, BCL2L3, MCL1L.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MFGLKRNAVI GLNLYCGGAG LGAGSGGATR PGGRLLATEK EASARREIGG GEAGAVIGGS AGASPPSTLT PDSRRVARPP PIGAEVPDVT ATPARLLFFA PTRRAAPLEE MEAPAADAIM SPEEELDGYE PEPLGKRPAV LPLLELVGES GNNTSTDGSL PSTPPPAEEE EDELYRQSLE IISRYLREQA TGAKDTKPMG RSGATSRKAL ETLRRVGDGV QRNHETAFQG MLRKLDIKNE DDVKSLSRVM IHVFSDGVTN WGRIVTLISF GAFVAKHLKT INQESCIEPL AESITDVLVR TKRDWLVKQR GWDGFVEFFH VEDLEGG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GREM1 HumanDescription:
GREM1 Human Recombinant
Gremlin-1 isoform 1, CKTSF1B1, DAND2, DRM, GREMLIN, IHG-2, PIG2, GREM1, Cell proliferation-inducing gene 2 protein, Cysteine knot superfamily 1, BMP antagonist 1, DAN domain family member 2, Down-regulated in Mos-transformed cells protein, Increased in high glucose protein 2.
Product # :
PRO-1359Price :
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Description
GREM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (25-184) and having a molecular mass of 20.7 kDa. GREM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GREM1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
GREM1 belongs to the BMP (bone morphogenic protein) antagonist family. Like BMPs, BMP antagonists comprise cystine knots and usually form homo- and heterodimers. The CAN (cerberus and dan) subfamily of BMP antagonists, to which GREM1 belongs, is characterized by a C-terminal cystine knot with an eight-membered ring. The antagonistic effect of the secreted glycosylated protein is because of its direct binding to BMP proteins. As an antagonist of BMP, GREM1 takes a place in regulating organogenesis, body patterning, and tissue differentiation. In mouse, GREM1 has been shown to convey the sonic hedgehog (SHH) signal from the polarizing region to the apical ectodermal ridge during limb bud outgrowth. Alternatively merged transcript variants encoding different isoforms have been found for this gene.
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Synonyms
Gremlin-1 isoform 1, CKTSF1B1, DAND2, DRM, GREMLIN, IHG-2, PIG2, GREM1, Cell proliferation-inducing gene 2 protein, Cysteine knot superfamily 1, BMP antagonist 1, DAN domain family member 2, Down-regulated in Mos-transformed cells protein, Increased in high glucose protein 2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSKKKGSQG AIPPPDKAQH NDSEQTQSPQ QPGSRNRGRG QGRGTAMPGE EVLESSQEAL HVTERKYLKR DWCKTQPLKQ TIHEEGCNSR TIINRFCYGQ CNSFYIPRHI RKEEGSFQSC SFCKPKKFTT MMVTLNCPEL QPPTKKKRVT RVKQCRCISI DLD.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IFNG HumanDescription:
IFN-Gamma Human Recombinant
Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.
Product # :
CYT-206Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- sds-page
Description
IFN-gamma Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 144 amino acids and having a molecular mass of 17kDa.The IFN-gamma is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 4.6.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined in a viral resistance assay is < 0.05 ng/ml, corresponding to a specific activity of 2.0 x 10,000,000 IU/mg.sds-page
More Info
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Introduction
IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I IFNs. -
Synonyms
Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IFN gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-gamma should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized IFN-gamma in sterile distilled water or 20mM AcOH not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFQGR RASQ.
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Background
IFN-gamma Human
About IFN-gamma Human:
IFN-gamma, often known as interferon gamma (and originally known as immune interferon), is a soluble, dimerized cytokine that is the only interferon in the type II class. Besides its primary function in preventing the spread of the vesicular stomatitis virus, interferon gamma release assays are extensively employed in the diagnosis of tuberculosis. IFN-gamma, encoded by the IFNG gene in humans, controls immunological responses by cell signaling, particularly through the JAK-STAT pathway. Subsequently, interferon gamma plays a crucial role in cancer immunotherapy by preventing tumor growth, managing immune defenses against pathogens and monitoring cells activity. In this article we will delve into the science behind IFN-gamma and explain its significance in biomedical research.
Description:
IFN-gamma Human Recombinant is a single non-glycosylated, polypeptide chain containing 144 amino acids and having a molecular mass of 17kDa that its original source is Escherichia Coli. This product appears as a sterile-filtered white lyophilized powder, ensuring purity and stability. Its formulation involves lyophilization from a filtered concentrated solution in PBS (pH 4.6). Its purity is determined both by analysis by RP-HPLC and SDS-PAGE and is therefore greater than 98%. In terms of stability, lyophilized IFN gamma is stable at room temperature for three weeks. However, it is preferable to store it desiccated below -18°C. In any case, you should prevent freeze thaw cycles. Additionally, reconstitution of IFN-gamma is recommended in sterile distilled water or 20mM AcOH, maintaining a concentration of at least 100µg/ml.
Protein Function:
Interferon gamma is a key player in immune control. It is a protein that plays a major role in complex cell signaling networks. The JAK-STAT pathway, which is essential for immunological regulation, is triggered by IFN-gamma through its interaction with the heterodimeric receptor. IFN-gamma's ability to regulate inflammation, apoptosis, cytokine signaling, and cell proliferation through protein mediated signaling skills is crucial for maintaining immune vigilance and response mechanisms. The incorporation of IFN-gamma into our product is validated by protein quantitation using two independent methods: UV spectroscopy and RP-HPLC.
Applications and Usage:
IFN-gamma Human is tailored for laboratory research, serving as a vital tool in elucidating immune mechanisms, exploring antiviral features, and unraveling tumor suppressor functions.
Safety Information:
IFN-gamma Human is only intended to be used in laboratory research, in line with safety protocols. It emphasizes adherence to ethical and regulatory norms and is not designed for use as household chemicals, pharmaceuticals, agricultural goods, or food additives.
What is the molecular weight/Mw of IFNG HUMAN Protein?
IFNG HUMAN Protein has a total Mw of 17kDa.
What is the source or expression system of IFNG HUMAN Protein?
Escherichia Coli.
What is the Purity of IFNG HUMAN Protein?
IFNG HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of IFNG HUMAN Protein?
The specific activity as determined in a viral resistance assay is < 0.05 ng/ml, corresponding to a specific activity of 2.0 x 10,000,000 IU/mg.
What is the amino acid sequence of IFNG HUMAN Protein?
MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFQGR RASQ.
What applications can IFNG HUMAN Protein be used in?
IFNG HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFNG HUMAN Protein?
The endotoxin level is minimal, IFNG HUMAN Protein was purified using conventional chromatography techniques.
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Protein content
Protein quantitation was carried out by two independent methods: 1. UV spectroscopy at 280 nm using the absorbency value of 0.640 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IFN-g as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SNUPN HumanDescription:
Snurportin 1 Human Recombinant
KPNBL, RNUT1, Snurportin1, SPN1, RNA U transporter 1.
Product # :
PRO-866Price :
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Shipped with Ice Packs
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Description
SNUPN Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 380 amino acids (1-360 a.a.) and having a molecular mass of 43.3 kDa. The SNUPN is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SNUPN Human solution containing 20mM Tris pH-8, 2mM DTT, 0.1M NaCl, & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
SNUPN is a nuclear import adaptor protein which is part of the Snurportin family.
SNUPN is Localized to the cytoplasm and nucleus and contains an N-terminal IBB domain and a trimethylguanosine (m3G)-cap binding domain. SNUPN binds specifically the terminal 2,2,7-m3G-cap at the 5'' end of U snRNPs and is involved in transport of U snRNPs into the nucleus through an association with Importin β. -
Synonyms
KPNBL, RNUT1, Snurportin1, SPN1, RNA U transporter 1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEELSQALAS SFSVSQDLNS TAAPHPRLSQ YKSKYSSLEQ SERRRRLLEL QKSKRLDYVN HARRLAEDDW TGMESEEENK KDDEEMDIDT VKKLPKHYAN QLMLSEWLID VPSDLGQEWI VVVCPVGKRA LIVASRGSTS AYTKSGYCVN RFSSLLPGGN RRNSTAKDYT ILDCIYNEVN QTYYVLDVMC WRGHPFYDCQ TDFRFYWMHS KLPEEEGLGE KTKLNPFKFV GLKNFPCTPE SLCDVLSMDF PFEVDGLLFY HKQTHYSPGS TPLVGWLRPY MVSDVLGVAV PAGPLTTKPD YAGHQLQQIM EHKKSQKEGM KEKLTHKASE NGHYELEHLS
TPKLKGSSHS PDHPGCLMEN.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
C17ORF103 HumanDescription:
Chromosome 17 Open Reading Frame 103 Human Recombinant
Chromosome 17 Open Reading Frame 103, Transcript Expressed During Hematopoiesis 2, Gene Trap Locus F3b, Gtlf3b, Protein GTLF3B.
Product # :
PRO-1619Price :
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Description
C17ORF103 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 136 amino acids (1-113) and having a molecular mass of 15.4kDa.C17ORF103 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The C17ORF103 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
C17orf103 is a member of the GTLF3B family and is encoded by a gene which is located in human chromosome 17p11.2. BRCA1 and p53 are 2 main tumor suppressor genes which are linked to chromosome 17. Tumor suppressor p53 is necessary for maintenance of cellular genetic integrity by moderating cell fate through DNA repair versus cell death. C17orf103 is also related to neurofibromatosis, a disorder characterized by neural and epidermal lesions, and dysregulated Schwann cell growth.
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Synonyms
Chromosome 17 Open Reading Frame 103, Transcript Expressed During Hematopoiesis 2, Gene Trap Locus F3b, Gtlf3b, Protein GTLF3B.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAHSAAA VPLGALEQGC PIRVEHDRRR RQFTVRLNGC HDRAVLLYEY VGKRIVDLQH TEVPDAYRGR GIAKHLAKAA LDFVVEEDLK AHLTCWYIQK YVKENPLPQY LERLQP
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HB-EGF HumanDescription:
HB-EGF Human Recombinant
HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.
Product # :
CYT-119Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
HB-EGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 87 amino acids and having a molecular mass of 9.9kDa. The HB-EGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM sodium phosphate pH-7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 106units/mg.
More Info
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Introduction
HB-EGF is an EGF related growth factor which signals via the EGF receptor, and stimulates the proliferation of SMC (smooth muscle cells), fibroblasts, epithelial cells and keratinocytes. HB-EGF is expressed in various cell types and tissues, including vascular endothelial cells and SMC, macrophages, skeletal muscle, keratinocytes and particular tumor cells. HB-EGF’s ability to explicitly bind HPR sulfate proteoglycans is dissimilar from other EGF-like molecules, and might be related to the enhanced mitogenic activity, relative to EGF, that HB-EGF exerts on smooth muscle cells.
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Synonyms
HBEGF, DTR, DTS, HEGFL, HB-EGF, Diphtheria toxin receptor, DT-R, DTSF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Human HB-EGF Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HB-EGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Human HB-EGF in sterile 18M-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC
KYVKELRAPS CICHPGYHGE RCHGLSL.
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Background
What is the molecular weight/Mw of HB-EGF Protein?
HB-EGF Protein has a total Mw of 9.9kDa.
What is the source or expression system of HB-EGF Protein?
Escherichia Coli.
What is the Purity of HB-EGF Protein?
HB-EGF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of HB-EGF Protein?
The ED50 was determined by the ability to induce proliferation of 3T3 cells and is 0.13-0.2ng/ml. This corresponds to an expected specific activity of 7.7 x 106units/mg.
What is the amino acid sequence of HB-EGF Protein?
MDLQEADLDL LRVTLSSKPQ ALATPNKEEH GKRKKKGKGL GKKRDPCLRK YKDFCIHGEC
KYVKELRAPS CICHPGYHGE RCHGLSL.
What applications can HB-EGF Protein be used in?
HB-EGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for HB-EGF Protein?
The endotoxin level is minimal, HB-EGF Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Adiponectin Human, HEKDescription:
Adiponectin Human Recombinant, HEK
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-434Price :
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Shipped at Room temp
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Description
Acrp30 Human Recombinant produced in HEK cells is a glycosylated polypeptide chain containing 234 amino acids (19-244a.a.) and having a molecular mass of 25.5kDa. Acrp30 is expressed with a FLAG tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
HEK293 (Human Embryonic Kidney cell line).
Formulation
Filtered (0.4µm) and lyophilized from 0.5mg/ml in 50mM phosphate Buffer, 75mM NaCl, pH 7.4.
Purity
Greater than 98% as determined by HPLC and SDS PAGE.
Biological Activity
In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.
sds-page
More Info
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Introduction
Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
For long term, store lyophilized AdipoQ at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C. The lyophilized protein remains stable for 24 months when stored at -20°C.
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Solubility
Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product not sterile! Please filter the product by an appropriate sterile filter before using it in cell culture.
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Amino Acid Sequence
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.
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Background
What is the molecular weight/Mw of adiponectin Protein?
Adiponectin Protein has a total Mw of 25.5kDa.
What is the source or expression system of adiponectin Protein?
HEK293.
What is the Purity of adiponectin Protein?
adiponectin Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of adiponectin Protein?
In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.
What is the amino acid sequence of adiponectin Protein?
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.
What applications can adiponectin Protein be used in?
adiponectin Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for adiponectin Protein?
The endotoxin level is minimal, adiponectin Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
FLT1 D7 HumanDescription:
Vascular Endothelial Growth Factor Receptor-1 D1-7 Human Recombinant
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
Product # :
PKA-241Price :
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Shipped at Room temp
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Description
Soluble FLT1 Human Recombinant fused with the Fc part of human IgG1 produced in baculovirus is disulfide-linked homodimeric, glycosylated, polypeptide containing 751 amino acids and having a molecular mass of 130 kDa. The soluble receptor protein contains only the first 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. The FLT1 fc/Chimera is purified by proprietary chromatographic techniques.
Source
Insect Cells.
Formulation
FLT1 D1-7 was lyophilized from a concentrated (1 mg/ml) sterile solution containing PBS Buffer, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The activity of FLT1/Fc was determined by its ability to inhibit the VEGF-dependent proliferation of human umbilical vein endothelial cells. The ED50 for this effect is typically 10-30 ng/ml, corresponding to a specific activity of 33,333.33-100,000 units/mg.More Info
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Introduction
Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.
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Synonyms
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized FLT-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution FLT1 should be stored at 4C between 2-7 days and for future use below -18C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized FLT1 Fc/Chimera in PBS not less than 50µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MVSYWDTGVL LCALLSCLLL TGSSSGSKLK DPELSLKGTQ HIMQAGQTLH LQCRGEAAHK WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN HTGFYSCKYL AVPTSKKKET ESAIYIFISD TGRPFVEMYS EIPEIIHMTE GRELVIPCRV TSPNITVTLK KFPLDTLIPD GKRIIWDSRK GFIISNATYK EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV KLLRGHTLVL NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK RSYRLSMKVK AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA GNYTILLSIK QSNVFKNLTA TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ ILTCTAYGIP QPTIKWFWHP CNHNHSEARC DFCSNNEESF ILDADSNMGN RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK VGTVGRNISF YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK KEITIRDQEA PYLLRNLSDH TVAISSSTTL DCHANGVPEP QITWFKNNHK IQQEPGIILG PGSSTLFIER VTEEDEGVYH CKATNQKGSV ESSAYLTVQG TAASDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI S.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MLANA HumanDescription:
Melan-A Human Recombinant
MART-1, MART1, Melanoma antigen recognized by T-cells 1, Antigen LB39-AA, Antigen SK29-AA, Protein Melan-A, MLANA.
Product # :
PRO-1498Price :
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Description
MLANA Human Recombinant produced in E. coli is a single polypeptide chain containing 94 amino acids (48-118) and having a molecular mass of 10.4kDa. MLANA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MLANA solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Melan-A (MLANA), is engaged in melanosome biogenesis by ensuring the stability of GPR143. MLANA takes part in the expression, stability, trafficking, and processing of melanocyte protein PMEL, which is essential to the formation of stage II melanosomes.
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Synonyms
MART-1, MART1, Melanoma antigen recognized by T-cells 1, Antigen LB39-AA, Antigen SK29-AA, Protein Melan-A, MLANA.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSCRRRNGY RALMDKSLHV GTQCALTRRC PQEGFDHRDS KVSLQEKNCE PVVPNAPPAY EKLSAEQSPP PYSP.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PAX8 HumanDescription:
Paired Box 8 Human Recombinant
Paired Box 8, Paired Box Gene 8, PAX8.
Product # :
PRO-2134Price :
Quantity :
Shipping Method :
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Description
PAX8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 310 amino acids (1-287 a.a) and having a molecular mass of 33.4kDa.PAX8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PAX8 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Paired box 8, also known as PAX8 functions in thyroid follicular cell development as well as in expression of thyroid-specific genes. PAX8 complexes with TTF-1& TTF-2 in order to stimulate thyroid follicular cell differentiation and thyroid hormone biosynthesis by regulating the expression of NIS (sodium iodide symporter) , TPO (thyroid peroxidase), TG (thyroglobulin) and the TSHR (thyrotropin receptor). Defects in PAX8 are the cause of CHNG2 (congenital hypothyroidism non-goitrous type 2).
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Synonyms
Paired Box 8, Paired Box Gene 8, PAX8.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPHNSIR SGHGGLNQLG GAFVNGRPLP EVVRQRIVDL AHQGVRPCDI SRQLRVSHGC VSKILGRYYE TGSIRPGVIG GSKPKVATPK VVEKIGDYKR QNPTMFAWEI RDRLLAEGVC DNDTVPSVSS INRIIRTKVQ QPFNLPMDSC VATKSLSPGH TLIPSSAVTP PESPQSDSLG STYSINGLLG IAQPGSDKRK MDDSDQDSCR LSIDSQSSSS GPRKHLRTDA FSQHHLEPLE CPFERQHYPE AYASPSHTKG EQEVNTLAMP MATPPTPPTA RPGASPTPAC
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
G CSF Human, HisDescription:
Granulocyte-Colony Stimulating Factor Human Recombinant, His Tag
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Product # :
CYT-476Price :
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Description
Granulocyte Colony Stimulating Factor-His Tag Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids, fragment (31-204) and having a molecular mass of 23.19 kDa with an amino-terminal hexahistidine tag.G-CSF-His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Granulocyte Colony Stimulating Factor His is supplied in 1x PBS and 50% glycerol.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Granulocyte Colony Stimulating Factor is a growth factor and/or cytokine produced by the endothelium, macrophages and a number of other immune cells. GCSF stimulates the bone marrow to produce granulocytes and also to stimulate the survival, proliferation, differentiation and function of neutrophil granulocyte progenator cells and mature neutrophils.
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Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
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Background
What is the molecular weight/Mw of G CSF Protein?
G CSF Protein has a total Mw of 23.19kDa.
What is the source or expression system of G CSF Protein?
Escherichia Coli.
What is the Purity of G CSF Protein?
G CSF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of G CSF Protein?
The biological functionality of G CSF Protein will be determined in the future.
What is the amino acid sequence of G CSF Protein?
G CSF Protein is composed from 174 amino acids.
What applications can G CSF Protein be used in?
G CSF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for G CSF Protein?
The endotoxin level is minimal, G CSF Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CGREF1 HumanDescription:
Cell Growth Regulator With EF-Hand Domain 1 Human Recombinant
Cell Growth Regulator With EF-Hand Domain 1, Cell Growth Regulatory Gene 11 Protein, Hydrophobestin, CGR11, Cell Growth Regulator With EF Hand Domain Protein 1, Cell Growth Regulator With EF Hand Domain 1, Cell growth regulator with EF hand domain protein 1.
Product # :
PRO-2154Price :
Quantity :
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Description
CGREF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 305 amino acids (20-301 a.a) and having a molecular mass of 32.3kDa. CGREF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CGREF1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH7.4).
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Cell Growth Regulator with EF-Hand Domain 1, also known as CGREF1 is a secreted calcium ion binding protein. CGREF1 includes two EF-hand domains & both EF-hands are essential for function. CGREF1 is most likely digested extracellularly by an unfamiliar serine protease generating extremely hydrophobic bioactive peptides. CGREF1 mediates cell-cell adhesion in a calcium-dependent manner. In addition, CGREF1 is capable to inhibit growth in more than a few cell lines.
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Synonyms
Cell Growth Regulator With EF-Hand Domain 1, Cell Growth Regulatory Gene 11 Protein, Hydrophobestin, CGR11, Cell Growth Regulator With EF Hand Domain Protein 1, Cell Growth Regulator With EF Hand Domain 1, Cell growth regulator with EF hand domain protein 1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSAPKDGVT RPDSEVQHQL LPNPFQPGQE QLGLLQSYLK GLGRTEVQLE HLSREQVLLY LFALHDYDQS GQLDGLELLS MLTAALAPGA ANSPTTNPVI LIVDKVLETQ DLNGDGLMTP AELINFPGVA LRHVEPGEPL APSPQEPQAV GRQSLLAKSP LRQETQEAPG PREEAKGQVE ARRESLDPVQ EPGGQAEADG DVPGPRGEAE GQAEAKGDAP GPRGEAGGQA EAEGDAPGPR GEAGGQAEAR ENGEEAKELP GETLESKNTQ NDFEVHIVQV ENDEI.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SNCA 61-140 HumanDescription:
Alpha Synuclein 61-140 Human Recombinant
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
Product # :
PRO-163Price :
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Description
A-Synuclein 61-140 Human Recombinant which is a deletion mutant of the a-synuclein amino acids 61-140 , produced in E.Coli is a single, non-glycosylated polypeptide chain of 81 amino acids having a molecular mass of 8.4kDa (molecular size on SDS-PAGE will appear higher), with an additional Met attached at the N-terminus. The Recombinant Human a-Synuclein 61-140 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SNCA 61-140 protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).
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Synonyms
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MEQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
AMH (452-560) HumanDescription:
Anti-Mullerian Hormone (452-560) Human Recombinant
Anti-Muellerian hormone, AMH, Muellerian-inhibiting substance, MIS, MIF.
Product # :
PRO-2843Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Anti-Mullerian Hormone Human Recombinant produced in CHO is a Homodimer, glycosylated, polypeptide chain containing 109 amino acids (Ser452-Arg560) and having a total molecular mass of 23.4Da.
Anti-Mullerian Hormone is purified by proprietary chromatographic techniques.
Source
CHO Cells.
Formulation
AMH Lyophilized from a 0.2µm filtered solution in 35% (v/v) Acetonitrile and 0.1% (v/v) TFA.
Purity
Greater than 97% as determined by SDS-PAGE and SEC-HPLC analyses.
Biological Activity
Immobilized Recombinant Human AMH at 3 µg/mL (100 µL/well) will bind Recombinant Human MIS RII Fc Chimera with a linear range of 2.0-100 ng/mL. The activity was measured by its binding ability in a functional ELISA.More Info
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Introduction
Anti-Mullerian Hormone also known as AMH is a member of the TGF-beta family. AMH is a glycoprotein which is produced by the Sertoli cells of the testis, causes regression of the Muellerian duct. AMH inhibits the growth of tumors derived from tissues of Muellerian duct origin. Moreover, AMH participates in Leydig cell differentiation and function in addition to follicular development in adult females.
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Synonyms
Anti-Muellerian hormone, AMH, Muellerian-inhibiting substance, MIS, MIF.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to reconstitute in sterile 4mM HCl to a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SAGATAADGP CALRELSVDL RAERSVLIPE TYQANNCQGV CGWPQSDRNP RYGNHVVLLL KMQVRGAALA RPPCCVPTAY AGKLLISLSE ERISAHHVPN MVATECGCR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
AGR2 HumanDescription:
Anterior Gradient Protein 2 Homolog Human Recombinant
Anterior gradient protein 2 homolog, Secreted cement gland protein XAG-2 homolog, AG-2, hAG-2, HPC8, AGR2, AG2, GOB-4, HAG-2, XAG-2.
Product # :
PRO-580Price :
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Description
AGR2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 191 amino acids (21-175 a.a.) and having a molecular mass of 21.9 kDa. AGR2 protein is fused to a 36 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
The protein contains 20mM Tris-HCl pH 8.0, 1mM DTT, 1mM EDTA and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
AGR2 (Anterior gradient 2 homolog) is the human orthologue of the secreted Xenopus laevis Anterior Gradient protein (XAG-2). This is a small, possibly secreted molecule of yet weakly defined functions that is widely expressed in human tissues. Expression of AGR2 shows a positive correlation with expression of estrogen receptor in breast carcinoma and a negative correlation with expression of EGF receptor.
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Synonyms
Anterior gradient protein 2 homolog, Secreted cement gland protein XAG-2 homolog, AG-2, hAG-2, HPC8, AGR2, AG2, GOB-4, HAG-2, XAG-2.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMRDT TVKPGAKKDT KDSRPKLPQT LSRGWGDQLI WTQTYEEALY KSKTSNKPLM IIHHLDECPH SQALKKVFAE NKEIQKLAEQ FVLLNLVYET TDKHLSPDGQ YVPRIMFVDP SLTVRADITG RYSNRLYAYE PADTALLLDN MKKALKLLKT EL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LECT1 (214-333) HumanDescription:
Leukocyte Cell Derived Chemotaxin 1 (214-333 a.a.) Human Recombinant
BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.
Product # :
PRO-1857Price :
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Description
LECT1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 143 amino acids (214-333) and having a molecular mass of 16.2kDa. LECT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LECT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Leukocyte Cell Derived Chemotaxin 1 (214-333 a.a.), also known as LECT1, is a glycosylated transmembrane protein which is cleaved to form a mature, secreted protein. The mature protein encourages chondrocyte growth and inhibits angiogenesis. The mature protein takes part in endochondral bone development by permitting cartilaginous anlagen to be vascularized and replaced by bone. LECT1 is expressed in the avascular area of prehypertrophic cartilage and its expression reduces during vascular invasion and chondrocyte hypertrophy.
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Synonyms
BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSREVVRKI VPTTTKRPHS GPRSNPGAGR LNNETRPSVQ EDSQAFNPDN PYHQEGESMT FDPRLDHEGI CCIECRRSYT HCQKICEPLG GYYPWPYNYQ GCRSACRVIM PCSWWVARIL GMV.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
VEGF (121 a.a.) Human, Sf9Description:
Vascular Endothelial Growth Factor (121 a.a.) Human Recombinant, Sf9
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
Product # :
CYT-200Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Vascular Endothelial Growth Factor-121 Human Recombinant produced in insect cells as an 18kDa homodimer, is a glycosylated, polypeptide chain containing 121 amino acids and having a molecular mass of approximately 36kDa.VEGF121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates.The VEGF-121 is purified by proprietary chromatographic techniques.
Source
Sf9, Insect Cells.
Formulation
The protein was lyophilized from a solution containing 50mM acetic acid.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using primary HUVECs. The ED50 for this effect is typically 2-10ng/ml.More Info
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Introduction
Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy. -
Synonyms
Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Vascular Endothelial Growth Factor 121 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-121 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
The lyophilized VEGF121 should be reconstituted in 50mM acetic acid to a concentration not lower than 50µg/ml.
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Amino Acid Sequence
APMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPS CVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHN KCECRPKKDRARQEKCDKPRR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CXCL6 HumanDescription:
Granulocyte Chemotactic Protein 2 (CXCL6) Human Recombinant
C-X-C motif chemokine 6, Chemokine alpha 3, CKA-3, Granulocyte chemotactic protein 2, GCP-2, Small-inducible cytokine B6.
Product # :
CHM-025Price :
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Shipping Method :
Shipped at Room temp
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Description
GCP-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 72 amino acids and having a molecular mass of 7.9kDa.
Source
Escherichia Coli.
Formulation
GCP-2 protein was lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration range of 10-50 ng/ml corresponding to a specific activity of 20,000-100,000 IU/mg.More Info
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Introduction
Granulocyte Chemotactic Protein 2 (CXCL6), also known as GCP-2, is a Chemotactic for neutrophil granulocytes. GCP-2 signals through binding and activation of its receptors (CXCR1 and CXCR2). GCP-2 has strong antibacterial activity against Gram-positive and Gram-negative bacteria In addition to its chemotactic and angiogenic property.
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Synonyms
C-X-C motif chemokine 6, Chemokine alpha 3, CKA-3, Granulocyte chemotactic protein 2, GCP-2, Small-inducible cytokine B6.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GCP-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GCP-2 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized GCP-2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
VLTELRCTCL RVTLRVNPKT IGKLQVFPAG PQCSKVEVVA SLKNGKQVCL DPEAPFLKKV IQKILDSGNK KN.
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Background
What is the molecular weight/Mw of CXCL6 HUMAN Protein?
CXCL6 HUMAN Protein has a total Mw of 7.9kDa.
What is the source or expression system of CXCL6 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL6 HUMAN Protein?
CXCL6 HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL6 HUMAN Protein?
Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration range of 10-50 ng/ml corresponding to a specific activity of 20,000-100,000 IU/mg.
What is the amino acid sequence of CXCL6 HUMAN Protein?
VLTELRCTCL RVTLRVNPKT IGKLQVFPAG PQCSKVEVVA SLKNGKQVCL DPEAPFLKKV IQKILDSGNK KN.
What applications can CXCL6 HUMAN Protein be used in?
CXCL6 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL6 HUMAN Protein?
The endotoxin level is minimal, CXCL6 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
LIF Human, Sf9Description:
Leukemia Inhibitory Factor Human Recombinant, Sf9
Leukemia Inhibitory Factor, Differentiation Inhibitory Activity, Cholinergic Differentiation Factor, Differentiation-Stimulating Factor, Hepatocyte-Stimulating Factor III, Differentiation-Inducing Factor, Melanoma-Derived LPL Inhibitor, Human Interleukin In DA Cells, D Factor, HILDA, MLPLI, Emfilermin, DIA, CDF, Leukemia inhibitory factor, LIF, Differentiation-stimulating factor, D factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin.
Product # :
CYT-1003Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LIF Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 189 amino acids (23-202a.a.) and having a molecular mass of 20.8kDa (Molecular size on SDS-PAGE will appear at approximately 18-40kDa). LIF is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
LIF protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using TF-1 human erythroleukemic cell. The ED50 for this effects is less or equal to 0.5 ng/ml.
More Info
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Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
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Synonyms
Leukemia Inhibitory Factor, Differentiation Inhibitory Activity, Cholinergic Differentiation Factor, Differentiation-Stimulating Factor, Hepatocyte-Stimulating Factor III, Differentiation-Inducing Factor, Melanoma-Derived LPL Inhibitor, Human Interleukin In DA Cells, D Factor, HILDA, MLPLI, Emfilermin, DIA, CDF, Leukemia inhibitory factor, LIF, Differentiation-stimulating factor, D factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPSPLPITP VNATCAIRHP CHNNLMNQIR SQLAQLNGSA NALFILYYTA QGEPFPNNLD KLCGPNVTDF PPFHANGTEK AKLVELYRIV VYLGTSLGNI TRDQKILNPS ALSLHSKLNA TADILRGLLS NVLCRLCSKY HVGHVDVTYG PDTSGKDVFQ KKKLGCQLLG KYKQIIAVLA
QAFHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CXCL6 BovineDescription:
Granulocyte Chemotactic Protein 2 (CXCL6) Bovine Recombinant
C-X-C motif chemokine 6, Chemokine alpha 3, CKA-3, Granulocyte chemotactic protein 2, GCP-2, Small-inducible cytokine B6.
Product # :
CHM-040Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Granulocyte Chemotactic Protein 2 (CXCL6) Bovine Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 76 amino acids and having a molecular mass of approximately 8.0kDa.GCP2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in 20 mM PB and 500mM NaCl, pH 7.0.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity determined by a chemotaxis bioassay using human neutrophils is 10-50 ng/ml.
More Info
-
Introduction
Granulocyte Chemotactic Protein 2 (CXCL6), also known as GCP-2, is a Chemotactic for neutrophil granulocytes. GCP-2 signals through binding and activation of its receptors (CXCR1 and CXCR2). GCP-2 has strong antibacterial activity against Gram-positive and Gram-negative bacteria in addition to its chemotactic and angiogenic property.
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Synonyms
C-X-C motif chemokine 6, Chemokine alpha 3, CKA-3, Granulocyte chemotactic protein 2, GCP-2, Small-inducible cytokine B6.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GCP2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Granulocyte Chemotactic Protein 2 (CXCL6) should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Granulocyte Chemotactic Protein 2 (CXCL6) in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
GPVAAVVREL RCVCLTTTPG IHPKTVSDLQ VIAAGPQCSK VEVIATLKNG REVCLDPEAP LIKKIVQKIL DSGKNN.
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Background
What is the molecular weight/Mw of CXCL6 BOVINE Protein?
CXCL6 BOVINE Protein has a total Mw of 8.0kDa.
What is the source or expression system of CXCL6 BOVINE Protein?
Escherichia Coli.
What is the Purity of CXCL6 BOVINE Protein?
CXCL6 BOVINE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL6 BOVINE Protein?
The biological activity determined by a chemotaxis bioassay using human neutrophils is 10-50 ng/ml.
What is the amino acid sequence of CXCL6 BOVINE Protein?
GPVAAVVREL RCVCLTTTPG IHPKTVSDLQ VIAAGPQCSK VEVIATLKNG REVCLDPEAP LIKKIVQKIL DSGKNN.
What applications can CXCL6 BOVINE Protein be used in?
CXCL6 BOVINE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL6 BOVINE Protein?
The endotoxin level is minimal, CXCL6 BOVINE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PI16 HumanDescription:
Peptidase Inhibitor 16 Human Recombinant
Peptidase inhibitor 16, PI-16, Cysteine-rich secretory protein 9, CRISP-9, PSP94-binding protein, PI16, CRISP9, PSPBP, MSMBBP, MGC45378, DKFZp586B1817.
Product # :
ENZ-113Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Peptidase Inhibitor 16 Human Recombinant is produced in HEK293 cells and fused with a C-terminal Flag Tag (11 amino acids). The PI16 Flag Tagged Fusion Protein is 45.7kDa protein containing a total of 426 amino acid residues and purified by proprietary chromatographic techniques.
Source
HEK293 (Human Embryonic Kidney cell line).
Formulation
PI16 was filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Peptidase Inhibitor 16 (PI16) which a member of the CRISP family, is a putative serine protease inhibitor. PI16 interacts with PSP94/MSMB. PI16 is expressed in the prostate, testis, ovary and intestine. It also concentrates in prostate cancer patient's sera. PI16 may serve as a marker following prostatectomy for prostate cancer.
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Synonyms
Peptidase inhibitor 16, PI-16, Cysteine-rich secretory protein 9, CRISP-9, PSP94-binding protein, PI16, CRISP9, PSPBP, MSMBBP, MGC45378, DKFZp586B1817.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized PI16 Human recombinant at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
LTDEEKRLMV ELHNLYRAQV SPPASDMLHM RWDEELAAFA KAYARQCVWG HNKERGRRGE NLFAITDEGM DVPLAMEEWH HEREHYNLSA ATCSPGQMCG HYTQVVWAKT ERIGCGSHFC EKLQGVEETN IELLVCNYEP PGNVKGKRPY QEGTPCSQCP SGYHCKNSLC EPIGSPEDAQ DLPYLVTEAP SFRATEASDS RKMGTPSSLA TGIPAFLVTE VSGSLATKAL PAVETQAPTS LATKDPPSMA TEAPPCVTTE VPSILAAHSL PSLDEEPVTF PKSTHVPIPK SADKVTDKTK VPSRSPENSL DPKMSLTGAR ELLPHAQEEA EAEAELPPSS EVLASVFPAQ DKPGELQATL DHTGHTSSKS LPNFPNTSAT ANATGGRALA LQSSLPGAEG PDKPSVVSGL NSGPGAAADYKDDDDK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GDNF HumanDescription:
Glial-Derived Neurotrophic Factor Human Recombinant
ATF1, ATF2, HFB1-GDNF, GDNF.
Product # :
CYT-305Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- sds-page
Description
Glial derived Neurotrophic Factor Human Recombinant produced in E.Coli is a non-glycosylated disulfide-linked homodimer containing 2 x 135 amino acids and having a total molecular mass of approximately 30kDa. GDNF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GDNF was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% Trehalose.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Biological Activity
The ED50 was determined by the proliferation of rat C6 cells is < 0.1 ng/ml, corresponding to a specific activity of > 1.0x107 units/mg.
sds-page
More Info
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Introduction
GDNF promotes the survival and differentiation of minergic neurons in culture, and is able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.
GDNF enhances survival and morphological differentiation of minergic neurons and increases their high-affinity uptake. -
Synonyms
ATF1, ATF2, HFB1-GDNF, GDNF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Glial-derived Neurotrophic Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDNF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Glial Derived Neurotrophic Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SPDKQMAVLP RRERNRQAAA ANPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCDAAETTYD KILKNLSRNR RLVSDKVGQA CCRPIAFDDD LSFLDDNLVY HILRKHSAKR CGCI.
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Background
What is the molecular weight/Mw of GDNF HUMAN Protein?
GDNF HUMAN Protein has a total Mw of 30kDa.
What is the source or expression system of GDNF HUMAN Protein?
Escherichia Coli.
What is the Purity of GDNF HUMAN Protein?
GDNF HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GDNF HUMAN Protein?
The ED50 was determined by the proliferation of rat C6 cells is < 0.1 ng/ml, corresponding to a specific activity of > 1.0x107 units/mg.
What is the amino acid sequence of GDNF HUMAN Protein?
SPDKQMAVLP RRERNRQAAA ANPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCDAAETTYD KILKNLSRNR RLVSDKVGQA CCRPIAFDDD LSFLDDNLVY HILRKHSAKR CGCI.
What applications can GDNF HUMAN Protein be used in?
GDNF HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDNF HUMAN Protein?
The endotoxin level is minimal, GDNF HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
S100P Human, HisDescription:
S100 Calcium Binding Protein P Human Recombinant, His Tag
Protein S100-E, S100E, Migration-Inducing Gene 9, MIG9.
Product # :
PRO-830Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
S100P Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 115 amino acids (1-95a.a.) and having a molecular mass of 12.6 kDa. S100P protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
S100P Human solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT, 0.05M NaCl & 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
S100P is a Ca2+ binding protein that is part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are found in the cytoplasm and/or nucleus of a large range of cells, and participates in the regulation of a number of cellular function such as cell cycle progression and differentiation. S100P participates in numerous biological functions but the exact functions or mechanism of its action is still mostly unknown. Once S100P binds calcium ions it goes through a conformational change that results in an exposure of a hydrophobic surface which permits the interaction with specific target proteins.
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Synonyms
Protein S100-E, S100E, Migration-Inducing Gene 9, MIG9.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTELETAMGM IIDVFSRYSG SEGSTQTLTK GELKVLMEKE LPGFLQSGKD KDAVDKLLKD LDANGDAQVD FSEFIVFVAA ITSACHKYFE KAGLK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.