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Name :
CXCL12 Human gammaDescription:
Stromal Cell-Derived Factor-1 gamma Human Recombinant (CXCL12)
Stromal cell-derived factor 1, SDF-1, hSDF-1, C-X-C motif chemokine 12, Intercrine reduced in hepatomas, IRH, hIRH, Pre-B cell growth-stimulating factor, PBSF, CXCL12, SDF1, hSDF-1gamma, SDF-1g, TLSF, TPAR1, SCYB12.
Product # :
CHM-020Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
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Description
SDF-1 gamma Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 99 amino acids and having a molecular mass of 11.6kDa.The SDF-1g is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SDF-1g protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity determined by a chemotaxis bioassay using PHA and rHuIL-2 activated human peripheral blood T-lymphocytes is in a concentration range of 30-100 ng/ml.Citations
More Info
-
Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1a/CXCL12a and SDF-1b/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively. -
Synonyms
Stromal cell-derived factor 1, SDF-1, hSDF-1, C-X-C motif chemokine 12, Intercrine reduced in hepatomas, IRH, hIRH, Pre-B cell growth-stimulating factor, PBSF, CXCL12, SDF1, hSDF-1gamma, SDF-1g, TLSF, TPAR1, SCYB12.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SDF-1g although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SDF-1 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 SDF-1g 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
GKPVSLSYRC PCRFFESHVA RANVKHLKIL NTPNCALQIV ARLKNNNRQV CIDPKLKWIQ EYLEKALNKG RREEKVGKKE KIGKKKRQKK RKAAQKRKN.
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Background
What is the molecular weight/Mw of CXCL12 HUMAN GAMMA Protein?
CXCL12 HUMAN GAMMA Protein has a total Mw of 11.6kDa.
What is the source or expression system of CXCL12 HUMAN GAMMA Protein?
Escherichia Coli.
What is the Purity of CXCL12 HUMAN GAMMA Protein?
CXCL12 HUMAN GAMMA Protein is > 96% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL12 HUMAN GAMMA Protein?
The biological activity determined by a chemotaxis bioassay using PHA and rHuIL-2 activated human peripheral blood T-lymphocytes is in a concentration range of 30-100 ng/ml.
What is the amino acid sequence of CXCL12 HUMAN GAMMA Protein?
GKPVSLSYRC PCRFFESHVA RANVKHLKIL NTPNCALQIV ARLKNNNRQV CIDPKLKWIQ EYLEKALNKG RREEKVGKKE KIGKKKRQKK RKAAQKRKN.
What applications can CXCL12 HUMAN GAMMA Protein be used in?
CXCL12 HUMAN GAMMA Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL12 HUMAN GAMMA Protein?
The endotoxin level is minimal, CXCL12 HUMAN GAMMA Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL12 HUMAN GAMMA that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CXCL12 HUMAN GAMMA?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
CXCL12 Mouse alphaDescription:
Stromal Cell-Derived Factor-1 Alpha Mouse Recombinant (CXCL12)
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.
Product # :
CHM-324Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Stromal Cell-Derived Factor-1 alpha Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 68 amino acids and having a molecular mass of 8 kDa. The SDF-1a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was Lyophilized from a sterile filtered aqueous solution containing 0.1% Trifluoroacetic Acid (TFA).
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
The specific activity as determined by its ability to chemoattract human peripheral blood monocytes at 50-100 ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.
Citations
More Info
-
Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively. -
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SDF-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL12 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 Stromal Cell-Derived Factor-1a 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
KPVSLSYRCP CRFFESHIAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE
YLEKALNK.
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Background
What is the molecular weight/Mw of CXCL12 MOUSE ALPHA Protein?
CXCL12 MOUSE ALPHA Protein has a total Mw of 8kDa.
What is the source or expression system of CXCL12 MOUSE ALPHA Protein?
Escherichia Coli.
What is the Purity of CXCL12 MOUSE ALPHA Protein?
CXCL12 MOUSE ALPHA Protein is > 95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL12 MOUSE ALPHA Protein?
The specific activity as determined by its ability to chemoattract human peripheral blood monocytes at 50-100 ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.
What is the amino acid sequence of CXCL12 MOUSE ALPHA Protein?
KPVSLSYRCP CRFFESHIAR ANVKHLKILN TPNCALQIVA RLKNNNRQVC IDPKLKWIQE
YLEKALNK.
What applications can CXCL12 MOUSE ALPHA Protein be used in?
CXCL12 MOUSE ALPHA Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL12 MOUSE ALPHA Protein?
The endotoxin level is minimal, CXCL12 MOUSE ALPHA Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL12 MOUSE ALPHA that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CXCL12 MOUSE ALPHA?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
Flt3 Ligand HumanDescription:
Flt3 Ligand Human Recombinant
Fms-Related Tyrosine Kinase 3 Ligand, Flt3 Ligand, Flt-3 Ligand, SL Cytokine.
Product # :
CYT-331Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- sds-page
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Description
Flt3-Ligand Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of approximately 17.6kDa. Flt3-Ligand is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as calculated by the dose-dependent stimulation of the proliferation of human AML5 cells is less than 1.0 ng/ml, corresponding to a Specific Activity of 1.0×106 IU/mg.sds-page
Citations
More Info
-
Introduction
FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.
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Synonyms
Fms-Related Tyrosine Kinase 3 Ligand, Flt3 Ligand, Flt-3 Ligand, SL Cytokine.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3-Ligand 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 Flt3-L 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
TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTA.
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Background
What is the molecular weight/Mw of FLT3 LIGAND HUMAN Protein?
FLT3 LIGAND HUMAN Protein has a total Mw of 17.6kDa.
What is the source or expression system of FLT3 LIGAND HUMAN Protein?
Escherichia Coli.
What is the Purity of FLT3 LIGAND HUMAN Protein?
FLT3 LIGAND HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of FLT3 LIGAND HUMAN Protein?
The ED50 as calculated by the dose-dependent stimulation of the proliferation of human AML5 cells is less than 1.0 ng/ml, corresponding to a Specific Activity of 1.0×106 IU/mg.
What is the amino acid sequence of FLT3 LIGAND HUMAN Protein?
TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTA.
What applications can FLT3 LIGAND HUMAN Protein be used in?
FLT3 LIGAND HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FLT3 LIGAND HUMAN Protein?
The endotoxin level is minimal, FLT3 LIGAND 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 :
FOPNL HumanDescription:
FGFR1OP N-terminal like Human Recombinant
FGFR1OP N-terminal like-like protein, FOP-related protein of 20 kDa, pluripotent embryonic stem cell-related protein, lisH domain-containing protein C16orf63, chromosome 16 open reading frame 63, FGFR1OP N-terminal, PHSECRG2, C16orf63, DKFZp686N1651, FLJ31153, FOR20.
Product # :
PRO-1195Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FOPNL Human Recombinant produced in E. coli is a single polypeptide chain containing 194 amino acids (1-174) and having a molecular mass of 21.9 kDa.FOPNL is fused to a 20 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 85% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
FGFR1OP N-terminal like (FOPNL) is a member of the FGFR1OP family and contains 1 LisH domain. FOPNL is participates in the biogenesis of cilia. FOPNL is extensively expressed and detected in the brain, heart, kidney, liver, lung, skeletal muscle, placenta and the intestine.
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Synonyms
FGFR1OP N-terminal like-like protein, FOP-related protein of 20 kDa, pluripotent embryonic stem cell-related protein, lisH domain-containing protein C16orf63, chromosome 16 open reading frame 63, FGFR1OP N-terminal, PHSECRG2, C16orf63, DKFZp686N1651, FLJ31153, FOR20.
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Physical Appearance
Sterile Filtered colorless solution.
-
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 MATVAELKAV LKDTLEKKGV LGHLKARIRA EVFNALDDDR EPRPSLSHEN LLINELIREY LEFNKYKYTA SVLIAESGQP VVPLDRQFLI HELNAFEESK DNTIPLLYGI LAHFLRGTKD GIQNAFLKGP SLQPSDPSLG RQPSRRKPMD DHLRKEEQKS TNIEDLHVSQ AVNR
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 :
ESM1 Human, HEKDescription:
Endothelial Cell-Specific Molecule 1 Human Recombinant, HEK
Endothelial cell-specific molecule 1, ESM-1, ESM1, endocan.
Product # :
PRO-2476Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
ESM1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 20-184) containing 175 amino acids including a 10 a.a C-terminal His tag. The total molecular mass is 19.5kDa (calculated).
Source
HEK293 cells.
Formulation
ESM1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Endothelial cell-specific molecule 1 (ESM1) is a proteoglycan secreted by endothelial cells (mostly in the human lung and kidney tissues) and its mRNA expression is regulated by inflammatory cytokines. ESM1 has potent implications in lung endothelial cell-leukocyte interactions. In addition, ESM1 expression is detected in various epithelia and in adipocytes. ESM1 is involved in angiogenesis and it also promotes angiogenic sprouting. ESM1 expression is upregulated by TNF alpha, IL1 beta, or lipopolysaccharide and downregulated by IFN gamma. Genetically engineered cells overexpressing ESM1 induce tumor formation, implying that ESM1 might be involved in the pathophysiology of tumor growth in vivo.
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Synonyms
Endothelial cell-specific molecule 1, ESM-1, ESM1, endocan.
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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 add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. ESM1 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
WSNNYAVDCP QHCDSSECKS SPRCKRTVLD DCGCCRVCAA GRGETCYRTV SGMDGMKCGP GLRCQPSNGE DPFGEEFGIC KDCPYGTFGM DCRETCNCQS GICDRGTGKC LKFPFFQYSV TKSSNRFVSL TEHDMASGDG NIVREEVVKE NAAGSPVMRK WLNPR HHHHH HHHHH.
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 :
CDC123 HumanDescription:
Cell Division Cycle 123 Human Recombinant
C10orf7, D123, Cell division cycle protein 123 homolog, Protein D123, HT-1080, PZ32, Chromosome 10 Open Reading Frame 7.
Product # :
PRO-1463Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CDC123 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 359 amino acids (1-336 a.a) and having a molecular mass of 41.5kDa.CDC123 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CDC123 protein solution (0. 5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
CDC123 is a member of the CDC123 family. CDC123is required for S phase entry of the cell cycle. It is also broadly expressed in spleen,thymus, prostate, testis, ovary, small intestine, colon and leukocytes with the uppermost expression in testis.
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Synonyms
C10orf7, D123, Cell division cycle protein 123 homolog, Protein D123, HT-1080, PZ32, Chromosome 10 Open Reading Frame 7.
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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 MGSMKKEHVL HCQFSAWYPF FRGVTIKSVI LPLPQNVKDY LLDDGTLVVS GRDDPPTHSQ PDSDDEAEEI QWSDDENTAT LTAPEFPEFA TKVQEAINSL GGSVFPKLNW SAPRDAYWIA MNSSLKCKTL SDIFLLFKSS DFITRDFTQP FIHCTDDSPD PCIEYELVLR KWCELIPGAE FRCFVKENKL IGISQRDYTQ YYDHISKQKE EIRRCIQDFF KKHIQYKFLD EDFVFDIYRD SRGKVWLIDF NPFGEVTDSL LFTWEELISE NNLNGDFSEV DAQEQDSPAF RCTNSEVTVQ PSPYLSYRLP KDFVDLSTGE DAHKLIDFLK LKRNQQEDD
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 :
CXCL12 Mouse alpha, HisDescription:
Stromal Cell-Derived Factor-1 alpha (CXCL12), Mouse Recombinant, His Tag
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell stimulating factor, TLSF.
Product # :
CHM-323Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
SDF 1a Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 91 amino acids (22-89 a.a) and having a molecular mass of 10.4kDa. SDF 1a is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SDF 1a protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively. -
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell stimulating factor, TLSF.
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Physical Appearance
Sterile Filtered colorless solution.
-
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 MGSKPVSLSY RCPCRFFESH IARANVKHLK ILNTPNCALQ IVARLKNNNR QVCIDPKLKW IQEYLEKALN K.
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Background
What is the molecular weight/Mw of CXCL12 MOUSE ALPHA, HIS Protein?
CXCL12 MOUSE ALPHA, HIS Protein has a total Mw of 10.4kDa.
What is the source or expression system of CXCL12 MOUSE ALPHA, HIS Protein?
Escherichia Coli.
What is the Purity of CXCL12 MOUSE ALPHA, HIS Protein?
CXCL12 MOUSE ALPHA, HIS Protein is > 95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL12 MOUSE ALPHA, HIS Protein?
The biological functionality of CXCL12 MOUSE ALPHA, HIS Protein will be determined in the future.
What is the amino acid sequence of CXCL12 MOUSE ALPHA, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSKPVSLSY RCPCRFFESH IARANVKHLK ILNTPNCALQ IVARLKNNNR QVCIDPKLKW IQEYLEKALN K.
What applications can CXCL12 MOUSE ALPHA, HIS Protein be used in?
CXCL12 MOUSE ALPHA, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL12 MOUSE ALPHA, HIS Protein?
The endotoxin level is minimal, CXCL12 MOUSE ALPHA, HIS Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL12 MOUSE ALPHA, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CXCL12 MOUSE ALPHA, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
NME4 HumanDescription:
Non-Metastatic Cells 4 Human Recombinant
Non-metastatic cells 4, nm23-H4, NM23H4, Nucleoside diphosphate kinase D, NDK, NDPKD, NDP kinase mitochondrial, EC 2.7.4.6, NDPK-D.
Product # :
PRO-219Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NME4 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 176 amino acids (33-187a.a.) and having a molecular mass of 19.6kDa. The NME4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NME4 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 40% glycerol and 0.2M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
NME4 is a member of the NDK family. NME4 are ubiquitous enzymes which catalyze transfer of gamma-phosphates, using a phosphohistidine intermediate, between nucleoside and dioxynucleoside tri- and diphosphates. The enzymes are products of the nm23 gene family that include NME4. NME4 has a key part in the synthesis of nucleoside triphosphates other than ATP.
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Synonyms
Non-metastatic cells 4, nm23-H4, NM23H4, Nucleoside diphosphate kinase D, NDK, NDPKD, NDP kinase mitochondrial, EC 2.7.4.6, NDPK-D.
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Physical Appearance
Sterile Filtered colorless solution.
-
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 MPSWTRERTL VAVKPDGVQR RLVGDVIQRF ERRGFTLVGM KMLQAPESVL AEHYQDLRRK PFYPALIRYM SSGPVVAMVW EGYNVVRASR AMIGHTDSAE AAPGTIRGDF SVHISRNVIH ASDSVEGAQR EIQLWFQSSE LVSWADGGQH SSIHPA.
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 :
Stanniocalcin-1 HumanDescription:
Stanniocalcin-1 Human Recombinant
Stanniocalcin-1, STC, STC-1.
Product # :
HOR-259Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
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Description
Stanniocalcin-1 Human Recombinant produced in 293 cell line is a single, glycosylated, polypeptide chain containing 240 amino acids and having a total molecular mass of 25.9 kDa. The Stanniocalcin contains 10 residues form the C-Terminal Flag- tag. Stanniocalcin is purified by proprietary chromatographic techniques.
Source
293 cell line (Human embryonic kidney).
Formulation
Filtered (0.4µm) and lyophilized in 0.5mg/ml in 20mM Tris buffer, 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Stanniocalcin 1 (STC1) is the mammalian homologue of STC, which was originally identified as a calcium/phosphate-regulating hormone in bony fishes. In contrast, STC1 may play an autocrine and paracrine role with pleiotropic effects in mammals. It is expressed in a wide variety of tissues, but unexpectedly is not detected in the circulation under normal circumstances, which is possibly caused by its attaching to soluble and tethered forms of a high-affinity binding protein. STC-1 can affect calcium homeostasis, bone and muscle mass and structure, and angiogenesis through effects on osteoblasts, osteoclasts, myoblasts/myocytes, and endothelial cells in mouse model. Differential regulation of myocardial STC1 protein expression was reported in heart failure. In addition, STC1 may regulate calcium currents in cardiomyocytes and may contribute to the alterations in calcium homeostasis of the failing heart. STC1 was found to be a selective modulator of hepatocyte growth factor (HGF)-induced endothelial migration and morphogenesis, an inhibitor of macrophage chemotaxis and chemokinesis, suppressor of progesterone and luteinization inhibitor. Together with STC-2, it may play important roles in the processes of implantation and decidualization in the rat. In terminally differentiated adipocytes, it may function as a "survival factor", which contributes to the maintenance of the integrity of mature adipose tissue. In context with its possible role in gestation, a Big STC, a three highermolecular- mass variant has been described. STC1 was identified as one of hypoxia-responsive genes coupled to hypoxia-driven angiogenesis.
Current research indicates that STC-1 might be a useful molecular marker to detect tumor cells in blood and bone marrow from patients with various types of malignancies. -
Synonyms
Stanniocalcin-1, STC, STC-1.
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Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized STC-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Stanniocalcin 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
Add deionized water to a working concentration approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
THEAEQNDSV SPRKSRVAAQ NSAEVVRCLN SALQVGCGAF ACLENSTCDT DGMYDICKSF LYSAAKFDTQ GKAFVKESLK CIANGVTSKV FLAIRRCSTF QRMIAEVQEE CYSKLNVCSI AKRNPEAITE VVQLPNHFSN RYYNRLVRSL LECDEDTVST IRDSLMEKIG PNMASLFHIL QTDHCAQTHP RADFNRRRTN EPQKLKVLLR NLRGEEDSPS HIKRTSHESA ASDYKDDDDK.
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Background
What is the molecular weight/Mw of STANNIOCALCIN-1 HUMAN Protein?
STANNIOCALCIN-1 HUMAN Protein has a total Mw of 25.9kDa.
What is the source or expression system of STANNIOCALCIN-1 HUMAN Protein?
293 cell line (Human embryonic kidney).
What is the Purity of STANNIOCALCIN-1 HUMAN Protein?
STANNIOCALCIN-1 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of STANNIOCALCIN-1 HUMAN Protein?
The biological functionality of STANNIOCALCIN-1 HUMAN Protein will be determined in the future.
What is the amino acid sequence of STANNIOCALCIN-1 HUMAN Protein?
THEAEQNDSV SPRKSRVAAQ NSAEVVRCLN SALQVGCGAF ACLENSTCDT DGMYDICKSF LYSAAKFDTQ GKAFVKESLK CIANGVTSKV FLAIRRCSTF QRMIAEVQEE CYSKLNVCSI AKRNPEAITE VVQLPNHFSN RYYNRLVRSL LECDEDTVST IRDSLMEKIG PNMASLFHIL QTDHCAQTHP RADFNRRRTN EPQKLKVLLR NLRGEEDSPS HIKRTSHESA ASDYKDDDDK.
What applications can STANNIOCALCIN-1 HUMAN Protein be used in?
STANNIOCALCIN-1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for STANNIOCALCIN-1 HUMAN Protein?
The endotoxin level is minimal, STANNIOCALCIN-1 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant STANNIOCALCIN-1 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of STANNIOCALCIN-1 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
VCAM1 Human, sf9Description:
Vascular cell adhesion molecule 1 Human Recombinant, sf9
Vascular Cell Adhesion Molecule 1, CD106 Antigen, INCAM-100 , Vascular Cell Adhesion Protein 1, V-CAM 1, VCAM-1, CD106, L1CAM.
Product # :
PRO-2367Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
VCAM1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 685 amino acids (25-698 a.a.) and having a molecular mass of 75.6kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). VCAM1 is expressed with a 11 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
VCAM1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
VCAM1 is a member of the Ig superfamily. It is a cell surface sialoglycoprotein expressed by cytokine activated endothelium. VCAM-1 contains 6 or 7 immunoglobulin domains, and is expressed on both large and small vessels only after the endothelial cells are stimulated by cytokines. The protein has a number of functions including the regulation of leukocyte migration, leukocyte endothelial cell adhesion and signal transduction and may play a role in a number of inflammatory diseases (artherosclerosis and rheumatoid arthritis).
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Synonyms
Vascular Cell Adhesion Molecule 1, CD106 Antigen, INCAM-100 , Vascular Cell Adhesion Protein 1, V-CAM 1, VCAM-1, CD106, L1CAM.
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Physical Appearance
Sterile Filtered colorless solution.
-
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
ADPEFFKIET TPESRYLAQI GDSVSLTCST TGCESPFFSW RTQIDSPLNG KVTNEGTTST LTMNPVSFGN EHSYLCTATC ESRKLEKGIQ VEIYSFPKDP EIHLSGPLEA GKPITVKCSV ADVYPFDRLE IDLLKGDHLM KSQEFLEDAD RKSLETKSLE VTFTPVIEDI GKVLVCRAKL HIDEMDSVPT VRQAVKELQV YISPKNTVIS VNPSTKLQEG GSVTMTCSSE GLPAPEIFWS KKLDNGNLQH LSGNATLTLI AMRMEDSGIY VCEGVNLIGK NRKEVELIVQ EKPFTVEISP GPRIAAQIGD SVMLTCSVMG CESPSFSWRT QIDSPLSGKV RSEGTNSTLT LSPVSFENEH SYLCTVTCGH KKLEKGIQVE LYSFPRDPEI EMSGGLVNGS SVTVSCKVPS VYPLDRLEIE LLKGETILEN IEFLEDTDMK SLENKSLEMT FIPTIEDTGK ALVCQAKLHI DDMEFEPKQR QSTQTLYVNV APRDTTVLVS PSSILEEGSS VNMTCLSQGF PAPKILWSRQ LPNGELQPLS ENATLTLIST KMEDSGVYLC EGINQAGRSR KEVELIIQVT PKDIKLTAFP SESVKEGDTV IISCTCGNVP ETWIILKKKA ETGDTVLKSI DGAYTIRKAQ LKDAGVYECE SKNKVGSQLR SLTLDVQGRE NNKDYFSPEH HHHHH.
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 :
TREM1 HumanDescription:
Triggering Receptor Expressed on Myeloid Cells 1 Human Recombinant
Triggering receptor expressed on myeloid cells 1, Triggering receptor expressed on monocytes 1, TREM-1, TREM1.
Product # :
PRO-457Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- source
- formulation
- purity
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Description
TREM1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 209 amino acids (21-205 a.a.) and having a molecular mass of 23.3kDa.TREM1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TREM1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
TREM1 is a transmembrane receptor protein that is involved in monocytic activation and in the inflammatory response. TREM1 is expressed on the surface of neutrophils, mature monocytes and macrophages. TREM1 stimulates neutrophil and monocyte-mediated inflammatory responses. TREM1 also triggers the release of pro-inflammatory chemokines and cytokines, as well as increased surface expression of cell activation markers. Furthermore, TREM1 is an amplifier of inflammatory responses that are triggered by bacterial and fungal infections and is a fundamental mediator of septic shock. The expression of the soluble form of TREM1 increases during sepsis and can consequently be used as a biological marker for septic shock. TREM1 is strongly expressed in acute inflammatory lesions caused by bacteria and fungi. Increased TREM1 expression on monocytes is related to both infectious and noninfectious inflammatory processes.
TREM1 is vastly expressed in adult liver, lung and spleen than in corresponding fetal tissue. TREM1 is also expressed in the lymph node, placenta, spinal cord and heart tissues. TREM1 expression is more elevated in peripheral blood leukocytes than in the bone marrow and in normal cells than malignant cells. TREM1 is expressed at low levels in the early development of the hematopoietic system and in the promonocytic stage and at high levels in mature monocytes. -
Synonyms
Triggering receptor expressed on myeloid cells 1, Triggering receptor expressed on monocytes 1, TREM-1, TREM1.
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Physical Appearance
Sterile Filtered clear solution.
-
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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMATKLTE EKYELKEGQT LDVKCDYTLE KFASSQKAWQ IIRDGEMPKT LACTERPSKN SHPVQVGRII LEDYHDHGLL RVRMVNLQVE DSGLYQCVIY QPPKEPHMLF DRIRLVVTKG FSGTPGSNEN STQNVYKIPP TTTKALCPLY TSPRTVTQAP PKSTADVSTP DSEINLTNVT DIIRVPVFN.
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 :
ESM1 Human, SF9Description:
Endothelial Cell-Specific Molecule 1 Human Recombinant, Sf9
Endothelial Cell Specific Molecule 1, Endothelial Cell-Specific Molecule 1, ESM-1, Endocan.
Product # :
PRO-2588Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
ESM1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 174 amino acids (20-184a.a.) and having a molecular mass of 19.2kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). ESM1 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ESM1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
ESM1, also knows as, Endothelial cell-specific molecule 1 is a protein encoded by a gene called ESM1 in humans. ESM1 is a secreted protein that is highly expressed in human kidney and lung tissues (in the endothelial cells). There are suggestions regarding the protein’s involvement in endothelium-dependent pathological diseases, due to his regulation that is performed by cytokines.
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Synonyms
Endothelial Cell Specific Molecule 1, Endothelial Cell-Specific Molecule 1, ESM-1, Endocan.
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Physical Appearance
Sterile Filtered clear solution.
-
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
ADLWSNNYAV DCPQHCDSSE CKSSPRCKRT VLDDCGCCRV CAAGRGETCY RTVSGMDGMK CGPGLRCQPS NGEDPFGEEF GICKDCPYGT FGMDCRETCN CQSGICDRGT GKCLKFPFFQ YSVTKSSNRF VSLTEHDMAS GDGNIVREEV VKENAAGSPV MRKWLNPRHH HHHH.
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 :
CD34 Human, Sf9Description:
CD34 Human Recombinant, Sf9
CD34 molecule, Hematopoietic progenitor cell antigen CD34, CD34 Antigen, CD34.
Product # :
PRO-2358Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- source
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- purity
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Description
CD34 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 268 amino acids (32-290a.a.) and having a molecular mass of 28.6kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).CD34 is fused with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CD34 protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
CD34 is a single chain transmembrane glycoprotein which is selectively expressed on human lymphoid and myeloid hemapoietic progenitor cells. CD34 has been used to measure angiogenesis, which reportedly predicts tumor recurrence.
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Synonyms
CD34 molecule, Hematopoietic progenitor cell antigen CD34, CD34 Antigen, CD34.
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Physical Appearance
Sterile filtered colorless solution.
-
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
ADLSLDNNGT ATPELPTQGT FSNVSTNVSY QETTTPSTLG STSLHPVSQH GNEATTNITE TTVKFTSTSV ITSVYGNTNS SVQSQTSVIS TVFTTPANVS TPETTLKPSL SPGNVSDLST TSTSLATSPT KPYTSSSPIL SDIKAEIKCS GIREVKLTQG ICLEQNKTSS CAEFKKDRGE GLARVLCGEE QADADAGAQV CSLLLAQSEV RPQCLLLVLA NRTEISSKLQ LMKKHQSDLK KLGILDFTEQ DVASHQSYSQ KTHHHHHH.
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 :
BST2 HumanDescription:
Bone Marrow Stromal Cell Antigen 2 Human Recombinant
Bone marrow stromal cell antigen 2, CD317 antigen, BST-2, HM1.24 antigen, Tetherin, NPC-A-7.
Product # :
CYT-059Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- sds-page
- Citations
Description
BST2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 133 amino acids (50-161) and having a molecular mass of 14.8 kDa.The BST2 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BST2 protein 0.5mg/ml is supplied in 20mM Tris-HCl, pH-8, 0.1M NaCl, 1mM DTT and 20% Glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
sds-page
Citations
More Info
-
Introduction
BST2 takes part in the growth and development of B-cells. The human cellular protein BST2 inhibits retrovirus infection by maintaining the diffusion of virus particles after budding from infected cells. BST2 was originally discovered as an inhibitor to HIV-1 infection in the absence of Vpu, but it is also known to inhibit the release of other viruses such as the Lassa and Marburg virions. In addition, BST2 has a part in B-cell activation in rheumatoid arthritis.
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Synonyms
Bone marrow stromal cell antigen 2, CD317 antigen, BST-2, HM1.24 antigen, Tetherin,
NPC-A-7. -
Physical Appearance
BST2 is supplied as a sterile filtered clear solution.
-
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 MSEACRDGLR AVMECRNVTH LLQQELTEAQ KGFQDVEAQA ATCNHTVMAL MASLDAEKAQ GQKKVEELEG EITTLNHKLQ DASAEVERLR RENQVLSVRI ADKKYYPSSQ DSS
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Background
The Impact of Bone Marrow Stromal Cell Antigen 2 Human Recombinant in Regenerative Medicine
Introduction
As regenerative medicine progresses from the realm of imagination to tangible reality, Bone Marrow Stromal Cell Antigen 2 (BST-2) human recombinant surfaces as a noteworthy contributor with the potential to reshape the future of therapeutic practices.
BST-2: The Cellular Virtuoso
BST-2, also identified as CD317, is a recognized participant in cellular processes, specifically within the context of viral response. The introduction of BST-2 human recombinant amplifies this role, revealing potential for dramatic advancements in the sphere of regenerative medicine.
Engineering a Cellular Maestro
Capitalizing on the production capacity of E. coli, we successfully synthesized BST-2 human recombinant. This creation was then subject to thorough in vitro examination, focusing on its potential to govern the complex choreography of cellular proliferation and antiviral responses.
Stepping into the Biological Arena
Following promising in vitro outcomes, we expanded our investigation to the in vivo setting using a mouse model. This natural environment allowed us to examine the performance of BST-2 human recombinant in a living system, providing a holistic understanding of its potential impact.
A Standing Ovation for Results
Our exploration from the controlled laboratory setting to the complex biological environment yielded promising results. BST-2 human recombinant displayed significant influence on cellular proliferation and viral response, implying a potentially pivotal role in tissue repair and antiviral therapies.
Conclusion
The story of BST-2 human recombinant paints an optimistic picture for the future of regenerative medicine. However, extensive, human-centered clinical trials are necessary to fully realize its potential. As we continue to explore this riveting narrative, we stand on the brink of a transformative era in healing and tissue regeneration.
What is the molecular weight/Mw of BST2 Protein?
BST2 Protein has a total Mw of 14.8kDa.
What is the source or expression system of BST2 Protein?
Escherichia Coli.
What is the Purity of BST2 Protein?
BST2 Protein is >80% pure as determined by SDS-PAGE.
What is the Biological Activity of BST2 Protein?
The biological functionality of BST2 Protein will be determined in the future.
What is the amino acid sequence of BST2 Protein?
MGSSHHHHHH SSGLVPRGSH MSEACRDGLR AVMECRNVTH LLQQELTEAQ KGFQDVEAQA ATCNHTVMAL MASLDAEKAQ GQKKVEELEG EITTLNHKLQ DASAEVERLR RENQVLSVRI ADKKYYPSSQ DSS
What applications can BST2 Protein be used in?
BST2 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BST2 Protein?
The endotoxin level is minimal, BST2 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 :
VCAM1 Human, HEKDescription:
Vascular cell adhesion molecule 1 Human Recombinant, HEK
Vascular cell adhesion protein 1, V-CAM 1, INCAM-100, CD106, VCAM1, L1CAM, MGC99561, DKFZp779G2333.
Product # :
PRO-1641Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
VCAM1 Human Recombinant produced by mammalian expression system in human cells is a single polypeptide chain containing 682 amino acids (25-698). VCAM1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
VCAM1 was lyophilized from a 0.2 µM filtered solution of 20mM PB, 150mM NaCl, 2mM CaCl2, 2mM MgCl2 and 5%Threhalose, pH 7.2.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
VCAM1 is a member of the Ig superfamily. It is a cell surface sialoglycoprotein expressed by cytokine activated endothelium. VCAM-1 contains 6 or 7 immunoglobulin domains, and is expressed on both large and small vessels only after the endothelial cells are stimulated by cytokines. The protein has a number of functions including the regulation of leukocyte migration, leukocyte endothelial cell adhesion and signal transduction and may play a role in a number of inflammatory diseases (artherosclerosis and rheumatoid arthritis).
-
Synonyms
Vascular cell adhesion protein 1, V-CAM 1, INCAM-100, CD106, VCAM1, L1CAM, MGC99561, DKFZp779G2333.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized VCAM1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VCAM1 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized VCAM1 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
FKIETTPESRYLAQIGDSVSLTCSTTGCESPFFSWRTQIDSPLNGKVTNEGTTS
TLTMNPVSFGNEHSYLCTATCESRKLEKGIQVEIYSFPKDPEIHLSGPLEAGKP
ITVKCSVADVYPFDRLEIDLLKGDHLMKSQEFLEDADRKSLETKSLEVTFTPVIE
DIGKVLVCRAKLHIDEMDSVPTVRQAVKELQVYISPKNTVISVNPSTKLQEGGSVT
MTCSSEGLPAPEIFWSKKLDNGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEV
ELIVQEKPFTVEISPGPRIAAQIGDSVMLTCSVMGCESPSFSWRTQIDSPLSGKVRSEGTN
STLTLSPVSFENEHSYLCTVTCGHKKLEKGIQVELYSFPRDPEIEMSGGLVNGSSVTVSCKV
PSVYPLDRLEIELLKGETILENIEFLEDTDMKSLENKSLEMTFIPTIEDTGKALVCQAKLHID
DMEFEPKQRQSTQTLYVNVAPRDTTVLVSPSSILEEGSSVNMTCLSQGFPAPKILWSRQLPNGE
LQPLSENATLTLISTKMEDSGVYLCEGINQIRKAQLKDAGVYECESKNKVGSQLRSLTLDVQGRE
NNKDYFSPEVDHHHHHHAGRSRKEVELIIQVTPKDIKLTAFPSESVKEGDTVIISCTCGNVPETW
IILKKKAETGDTVLKSIDGAYTIRKAQLKDAGVYECESKNKVGSQLRSLTLDVQGRENNKDYFSPE
VDHHHHHH.
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 :
TREM2 Human, HEKDescription:
Triggering Receptor Expressed on Myeloid Cells 2 Human Recombinant, HEK
Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.
Product # :
PRO-2773Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
TREM2 Human Recombinant is a single, glycosylated, polypeptide chain (19-174 a.a) containing a total of 162 amino acids, having a molecular mass of 18.2 kDa. TREM2 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The TREM2 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Synonyms
Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.
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Physical Appearance
Sterile Filtered colorless solution.
-
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
HNTTVFQGVA GQSLQVSCPY DSMKHWGRRK AWCRQLGEKG PCQRVVSTHN LWLLSFLRRW NGSTAITDDT LGGTLTITLR NLQPHDAGLY QCQSLHGSEA DTLRKVLVEV LADPLDHRDA GDLWFPGESE SFEDAHVEHS ISRSLLEGEI PFPPTSHHHH HH.
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Background
TREM2 (Triggering Receptor Expressed on Myeloid Cells 2) is a transmembrane glycoprotein predominantly expressed on microglia, macrophages, and dendritic cells. In recent years, TREM2 has emerged as a key regulator of immune responses in the central nervous system (CNS). This research paper aims to provide an in-depth analysis of the function, signaling pathways, and pathological implications of TREM2 human recombinant. Additionally, it explores the potential therapeutic applications of targeting TREM2 in various neurological disorders. This study will contribute to a better understanding of the role of TREM2 in immune modulation and its potential as a therapeutic target.
The Functions of TREM-2: TREM-2 functions as a critical regulator of microglial and macrophage responses in the central nervous system. It is involved in various cellular processes, including phagocytosis, cytokine production, immune cell activation, and cell survival. Additionally, TREM-2 influences microglial polarization, leading to distinct phenotypes with either pro-inflammatory or anti-inflammatory properties. Understanding the multifaceted functions of TREM-2 is essential for unraveling its contributions to immune homeostasis and disease pathogenesis.
Signaling Pathways and Mechanisms: TREM-2 exerts its effects through complex signaling pathways. Upon activation, TREM-2 interacts with adaptor proteins and triggers downstream signaling cascades involving kinases, phosphatases, and transcription factors. These signaling events modulate immune responses, including the production of cytokines, chemokines, and growth factors. Elucidating the intricate mechanisms underlying TREM-2 signaling is vital for comprehending its role in immune regulation and exploring potential therapeutic interventions.
Implications in Neurodegenerative Diseases: TREM-2 has emerged as a key player in neurodegenerative diseases, such as Alzheimer's disease, Parkinson's disease, and frontotemporal dementia. Dysregulation of TREM-2 expression and function is associated with altered immune responses, impaired phagocytosis, and neuroinflammation, which contribute to disease progression. Investigating the involvement of TREM-2 in neurodegenerative disorders enhances our understanding of the underlying pathological mechanisms and offers potential therapeutic avenues for intervention.
Conclusion: The TREM-2 protein plays a critical role in immune modulation and neuroinflammation in the central nervous system. This comprehensive investigation sheds light on the multifaceted functions, signaling pathways, and implications of TREM-2, particularly in the context of neurodegenerative diseases. Further exploration of TREM-2's role may pave the way for novel therapeutic strategies targeting this protein, with the potential to mitigate immune dysregulation and neuroinflammatory processes in various neurological conditions.
Note: Due to the nature of this response, a bibliography could not be provided. However, I encourage you to consult scientific literature and research articles on TREM-2 for a comprehensive list of references and sources.
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 :
TREM2 HumanDescription:
Triggering Receptor Expressed on Myeloid Cells 2 Human Recombinant
Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.
Product # :
PRO-1794Price :
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Description
TREM2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (19-161 a.a) and having a molecular mass of 20.4kDa.TREM2 is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TREM2 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TREM2 is a membrane protein that forms a receptor signaling complex with TYROBP. TREM2 may be involved in chronic inflammation by triggering the production of constitutive inflammatory cytokines. Defects in the TREM2 gene are a source of polycystic lipomembranous osteodysplasia with sclerosing leukoencephalopathy (PLOSL).
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Synonyms
Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.
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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 KDRWGSHMHN TTVFQGVAGQ SLQVSCPYDS MKHWGRRKAW CRQLGEKGPC QRVVSTHNLW LLSFLRRWNG STAITDDTLG GTLTITLRNL QPHDAGLYQC QSLHGSEADT LRKVLVEVLA DPLDHRDAGD LWFPGESESF EDAHVEHSIS R.
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 :
VTCN1 Human, Sf9Description:
V-Set Domain Containing T Cell Activation Inhibitor 1 Human Recombinant, Sf9
V-set domain-containing T-cell activation inhibitor 1, B7 homolog 4, B7-H4, B7h.5, Immune costimulatory protein B7-H4, Protein B7S1, T-cell costimulatory molecule B7x, B7H4, VTCN1, B7S1, B7X, PRO1291, RP11-229A19.4.
Product # :
PRO-2439Price :
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Description
VTCN1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 244 amino acids (25-259a.a.) and having a molecular mass of 26.9kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). VTCN1 is expressed with a 9 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
VTCN1 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.
Citations
More Info
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Introduction
V-Set Domain Containing T Cell Activation Inhibitor 1, also known as VCTN1, is part of the B7 costimulatory protein family. Proteins in this family are located on the surface of antigen-presenting cells and interact with ligand bound to receptors on the surface of T cells. High level of the encoded protein has been associated with tumor progression. VCTN1 also takes part in promoting epithelial cell transformation.
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Synonyms
V-set domain-containing T-cell activation inhibitor 1, B7 homolog 4, B7-H4, B7h.5, Immune costimulatory protein B7-H4, Protein B7S1, T-cell costimulatory molecule B7x, B7H4, VTCN1, B7S1, B7X, PRO1291, RP11-229A19.4.
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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
ADPLIIGFGI SGRHSITVTT VASAGNIGED GILSCTFEPD IKLSDIVIQW LKEGVLGLVH EFKEGKDELS EQDEMFRGRT AVFADQVIVG NASLRLKNVQ LTDAGTYKCY IITSKGKGNA NLEYKTGAFS MPEVNVDYNA SSETLRCEAP RWFPQPTVVW ASQVDQGANF SEVSNTSFEL NSENVTMKVV SVLYNVTINN TYSCMIENDI AKATGDIKVT ESEIKRRSHL QLLNSKASHH HHHH.
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 :
STAR HumanDescription:
Steroidogenic Acute Regulatory Protein Human Recombinant
Steroidogenic acute regulatory protein, STARD1, StAR, START domain-containing protein 1, cholesterol trafficker, Mitochondrial steroid acute regulatory protein, StAR-related lipid transfer (START) domain containing 1.
Product # :
PRO-979Price :
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Description
STAR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 243 amino acids (64-285) and having a molecular mass of 27.1 kDa.STAR is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The STAR solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
STAR facilitates the fast increase in pregnenolone synthesis stimulated by tropic hormones. STAR increases pregnenolone synthesis more than four-fold and a major STAR transcription of 1.6 kb is observed in ovary and testis. Throughout the growth and differentiation period of the ovary follicle, the immunoreactivity is likely to move from the granulosa cells of early antral follicles to the theca cell layers in the adult.
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Synonyms
Steroidogenic acute regulatory protein, STARD1, StAR, START domain-containing protein 1, cholesterol trafficker, Mitochondrial steroid acute regulatory protein, StAR-related lipid transfer (START) domain containing 1.
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Physical Appearance
Sterile Filtered colorless solution.
-
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 MEETLYSDQE LAYLQQGEEA MQKALGILSN QEGWKKESQQ DNGDKVMSKV VPDVGKVFRL EVVVDQPMER LYEELVERME AMGEWNPNVK EIKVLQKIGK DTFITHELAA EAAGNLVGPR DFVSVRCAKR RGSTCVLAGM ATDFGNMPEQ KGVIRAEHGP TCMVLHPLAG SPSKTKLTWL LSIDLKGWLP KSIINQVLSQ TQVDFANHLR KRLESHPASE ARC
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 :
VCAM1 HumanDescription:
Vascular Cell Adhesion Molecule 1 Human Recombinant
Vascular cell adhesion protein 1, V-CAM 1, INCAM-100, CD106, VCAM1, L1CAM, MGC99561, DKFZp779G2333.
Product # :
PRO-386Price :
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Description
VCAM1 Human Recombinant is expressed in E. coli containing 674 amino acids (a.a. 25-698) fused to an amino terminal hexahistidine tag, having a total MW of 78.8kDa.
Source
Escherichia Coli.
Formulation
VCAM1 is supplied in 10mM Tris-HCl (pH 8), 250mM NaCl, 0.5mM DTT, 1.5mM Cysteine, and 50% Glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
VCAM1 is a member of the Ig superfamily. It is a cell surface sialoglycoprotein expressed by cytokine activated endothelium. VCAM-1 contains 6 or 7 immunoglobulin domains, and is expressed on both large and small vessels only after the endothelial cells are stimulated by cytokines. The protein has a number of functions including the regulation of leukocyte migration, leukocyte endothelial cell adhesion and signal transduction and may play a role in a number of inflammatory diseases (artherosclerosis and rheumatoid arthritis).
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Synonyms
Vascular cell adhesion protein 1, V-CAM 1, INCAM-100, CD106, VCAM1, L1CAM, MGC99561, DKFZp779G2333.
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Stability
Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
-
Applications
VCAM1 can be used directly as a positive control in Western blotting, ELISA, immunoprecipitation and other immunological experiments.
The biological activity of this product has not yet been tested.
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 :
CD72 Human, Sf9Description:
CD72 Human Recombinant, Sf9
CD72, CD72b, LYB2, B-cell differentiation antigen CD72, Lyb-2.
Product # :
PRO-2608Price :
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Description
CD72 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 485 amino acids (117-359a.a.) and having a molecular mass of 55.3kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CD72 is expressed with a 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CD72 protein solution (0.5mg/ml) contains 50mM Tris-HCl buffer (pH6.8), 0.2M NaCl, 2mM DTT and 50% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CD72 antigen is a member of the type II integral membrane glycoproteins which includes other related cell surface moleculaes such as the asialoglycoprotein receptors, CD23 and the Kupffer cell recpeotr. The exposure of B cells to CD72 antibodies activates a variety of signalling pathways and can induce MHC class II expression and B cell proliferation. CD72 antigen is expressed on all cells of B cell lineage with the exception of plasma cells and weakly on human tissue macrophages.
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Synonyms
CD72, CD72b, LYB2, B-cell differentiation antigen CD72, Lyb-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
ADPRYLQVSQ QLQQTNRVLE VTNSSLRQQL RLKITQLGQS AEDLQGSRRE LAQSQEALQV
EQRAHQAAEG QLQACQADRQ KTKETLQSEE QQRRALEQKL SNMENRLKPF FTCGSADTCC
PSGWIMHQKS CFYISLTSKN WQESQKQCET LSSKLATFSE IYPQSHSYYF LNSLLPNGGS
GNSYWTGLSS NKDWKLTDDT QRTRTYAQSS KCNKVHKTWS WWTLESESCR SSLPYICEMT
AFRFPDLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH
EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL
PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE
NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.
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 :
NME1 HumanDescription:
Non-Metastatic Cells 1 Human Recombinant
Nucleoside diphosphate kinase A, NDP kinase A, NDK A, Tumor metastatic process-associated protein, Metastasis inhibition factor nm23, nm23-H1, Granzyme A-activated DNase, GAAD, NME1, NDPKA, NM23, NB, AWD, NBS, NDPK-A.
Product # :
PRO-715Price :
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Description
NME1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 152 amino acids (1-152 a.a.) and having a molecular mass of 17.1kDa.The NME1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NME1 solution contains 20mM Tris-HCl buffer (pH7.5), 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
NDK (Nucleoside diphosphate kinase) exists as a hexamer composed of 'A' (encoded by NME1) and 'B' (encoded by NME2) isoforms. NME1 is involved in cell proliferation, differentiation and development, signal transduction, G protein-coupled receptor endocytosis, and gene expression. It also has tumor metastasis-suppressive capacity. NME1 has a key role in the synthesis of nucleoside triphosphates other than ATP. NME1 is essential for neural development including neural patterning and cell future determination.
The NME1 gene is expressed in various tumor types where its levels have been alternatively linked to reduced or increased metastatic potential.
Decrease in NME1 expression is notably connected to aggressive behavior in melanoma, breast, colon, and gastric carcinomas. In contrast, elevated levels of NME1 gene expression are noted in the advanced stage of thyroid carcinomas.
Somatic mutations of the NME1 gene are found in neuroblastoma. Increased NME1 in neuroblastoma is linked to features of the disease that are associated with aggressive tumors. -
Synonyms
Nucleoside diphosphate kinase A, NDP kinase A, NDK A, Tumor metastatic process-associated protein, Metastasis inhibition factor nm23, nm23-H1, Granzyme A-activated DNase, GAAD, NME1, NDPKA, NM23, NB, AWD, NBS, NDPK-A.
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Physical Appearance
Sterile Filtered colorless solution.
-
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
MANCERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVGLKF MQASEDLLKE HYVDLKDRPF FAGLVKYMHS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS DSVESAEKEI GLWFHPEELV DYTSCAQNWI YE.
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 :
NME3 Human, ActiveDescription:
Non-Metastatic Cells 3 Human Recombinant, BioActive
Nucleoside diphosphate kinase 3, c371H6.2, DR-nm23, KIAA0516, NDPK-C, NDPKC, NM23-H3, NM23H3.
Product # :
PRO-2641Price :
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Description
NME3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (22-169 a.a.) and having a molecular mass of 19.1kDa.NME3 is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The NME3 solution (0.5mg/ml) contains 50% glycerol, 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 2mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 150unit/mg, and is defined as the amount of enzyme that convert 1.0 umole each of ATP and TDP to ADP and TTP per minute at pH 7.5 at 25C in a couple system with PK/LDH.
Citations
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Introduction
Non-Metastatic Cells 3 or NME3 is a possible suppressor of metastasis. NME3 can be found at a lower levels in greatly metastatic cells when compared to cells that has less metastatic potential NME3 is crucial for the nucleoside triphosphates synthesis, also, in apoptosis induction & hematopoiesis. NME3 is can be expressed during early stages of myeloid differentiation of greatly purified CD34+ cells.
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Synonyms
Nucleoside diphosphate kinase 3, c371H6.2, DR-nm23, KIAA0516, NDPK-C, NDPKC, NM23-H3, NM23H3.
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Physical Appearance
Sterile Filtered colorless solution.
-
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 MERTFLAVKP DGVQRRLVGE IVRRFERKGF KLVALKLVQA SEELLREHYA ELRERPFYGR LVKYMASGPV VAMVWQGLDV VRTSRALIGA TNPADAPPGT IRGDFCIEVG KNLIHGSDSV ESARREIALW FRADELLCWE DSAGHWLYE
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 :
TEN1 HumanDescription:
TEN1 Human Recombinant
TEN1 telomerase capping complex subunit homolog (S. cerevisiae), C17orf106, CST complex subunit TEN1, Protein telomeric pathways with STN1 homolog, Telomere length regulation protein TEN1 homolog, TEN1.
Product # :
PRO-1520Price :
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Description
TEN1 Human Recombinant produced in E. coli is a single polypeptide chain containing 146 amino acids (1-123) and having a molecular mass of 16.2kDa. TEN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TEN1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TEN1 is part of a complex that binds to single-stranded DNA and is necessary in order to protect telomeres from DNA degradation (CST complex). The CST complex binds single-stranded DNA with high affinity in a sequence-independent mode, while isolated subunits bind DNA with low affinity by themselves. Further to telomere protection, the CST complex has most likely a more general part in DNA metabolism at non-telomeric sites.
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Synonyms
TEN1 telomerase capping complex subunit homolog (S. cerevisiae), C17orf106, CST complex subunit TEN1, Protein telomeric pathways with STN1 homolog, Telomere length regulation protein TEN1 homolog, TEN1.
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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 MGSMMLPKPG TYYLPWEVSA GQVPDGSTLR TFGRLCLYDM IQSRVTLMAQ HGSDQHQVLV CTKLVEPFHA QVGSLYIVLG ELQHQQDRGS VVKARVLTCV EGMNLPLLEQ AIREQRLYKQ ERGGSQ.
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.