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1000 results found for “calcyphosine”
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Name :
CXCL16 MouseDescription:
CXCL16 Mouse Recombinant
C-X-C motif chemokine 16, Small-inducible cytokine B16, Transmembrane chemokine CXCL16, Scavenger receptor for phosphatidylserine and oxidized low density lipoprotein, SR-PSOX, Cxcl16, Srpsox, Zmynd15, AV290116, BB024863, 0910001K24Rik.
Product # :
CHM-363Price :
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Shipped at Room temp
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Description
CXCL16 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 88 amino acids and having a molecular mass of 9.9kDa. The CXCL16 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 50mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract murine lymphocytes using a concentration range of 100-1000ng/ml corresponding to a Specific Activity of 1,000-10,000IU/mg.More Info
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Introduction
Mouse CXCL16 is a nonELR motif including CXC chemokine with a transmembrane domain. Mouse CXCL16 cDNA encodes a 246 a.a. precursor protein with a putative 26 a.a. residue signal peptide, an 88 a.a. residue chemokine domain, an 87 a.a. residue mucinlike spacer region, a 22 a.a. residue transmembrane domain, and a 23 a.a. residue cytoplasmic tail.
CXCL16 induces a strong chemotactic response and calcium mobilization. Furthermore, CXCL16 acts as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), suggesting that it may be involved in pathophysiology such as atherogenesis.
Mouse CXCL16 is generated by dendritic cells in lymphoid organ T cell zones as well as by cells in the splenic red pulp both as membranebound and soluble forms. CXCR6/Bonzo (STRL33 and TYMSTR) is the receptor for CXCL16. CXCL16 is expressed in the spleen, lymph nodes, and Peyer patches. It is also expressed in non-lymphoid tissues such as lung, kidney, small intestine, and thymus, with weak expression in heart and liver and no expression in brain and purified B- and T-cells.
CXCL16 deficiency is linked to breast cancer progression. In addition, CXCL16 is involved in immunological liver injury by regulating T lymphocyte infiltration in liver tissue. Furtheremore, CXCL16 has a distinctive role in the maintenance of cardiac allograft tolerance mediated by natural killer T cells. Moreover, CXCL16 has a significant role in not only the production of IFN-gamma by NKT cells, but also promotion of Th1-inclined immune responses mediated by NKT cells. -
Synonyms
C-X-C motif chemokine 16, Small-inducible cytokine B16, Transmembrane chemokine CXCL16, Scavenger receptor for phosphatidylserine and oxidized low density lipoprotein, SR-PSOX, Cxcl16, Srpsox, Zmynd15, AV290116, BB024863, 0910001K24Rik.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CXCL16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL16 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 CXCL16 Mouse 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
NQGSVAGSCS CDRTISSGTQ IPQGTLDHIR KYLKAFHRCP FFIRFQLQSK SVCGGSQDQW VRELVDCFER KECGTGHGKS FHHQKHLP.
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Background
What is the molecular weight/Mw of CXCL16 MOUSE Protein?
CXCL16 MOUSE Protein has a total Mw of 9.9kDa.
What is the source or expression system of CXCL16 MOUSE Protein?
Escherichia Coli.
What is the Purity of CXCL16 MOUSE Protein?
CXCL16 MOUSE Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL16 MOUSE Protein?
Determined by its ability to chemoattract murine lymphocytes using a concentration range of 100-1000ng/ml corresponding to a Specific Activity of 1,000-10,000IU/mg.
What is the amino acid sequence of CXCL16 MOUSE Protein?
NQGSVAGSCS CDRTISSGTQ IPQGTLDHIR KYLKAFHRCP FFIRFQLQSK SVCGGSQDQW VRELVDCFER KECGTGHGKS FHHQKHLP.
What applications can CXCL16 MOUSE Protein be used in?
CXCL16 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL16 MOUSE Protein?
The endotoxin level is minimal, CXCL16 MOUSE 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 :
Cyclophilin F RatDescription:
Cyclophilin F Rat Recombinant
Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase F, Cyclophilin D, CyP-D, CypD, Cyclophilin F, Rotamase F, Ppif, Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase.
Product # :
ENZ-903Price :
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Shipped with Ice Packs
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Description
Cyclophilin F Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids (30-206a.a.) and having a molecular mass of 21.2kDa.Cyclophilin F is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Cyclophilin F protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Peptidyl-prolyl cis-trans isomerase F, mitochondrial (Cyclophilin-F) accelerates the folding of proteins. Cyclophilin-F catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and involved in regulation of the mitochondrial permeability transition pore (mPTP). Cyclophilin-F, in cooperation with mitochondrial TP53, is involved in activating oxidative stress-induced necrosis. Cyclophilin-F is also involved in modulation of mitochondrial membrane F1F0 ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Furthermore, Cyclophilin-F has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis.
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Synonyms
Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase F, Cyclophilin D, CyP-D, CypD, Cyclophilin F, Rotamase F, Ppif, Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase.
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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 MGSCSDGGAR GANSSSQNPL VYLDVGADGQ PLGRVVLELK ADVVPKTAEN FRALCTGEKG FGYKGSTFHR VIPAFMCQAG DFTNHNGTGG KSIYGSRFPD ENFTLKHVGP GVLSMANAGP NTNGSQFFIC TIKTDWLDGK HVVFGHVKEG MDVVKKIESF GSKSGKTSKK IVITDCGQLS.
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 :
CYTH1 HumanDescription:
Cytohesin 1 Human Recombinant
Cytohesin 1, D17S811E, PH, SEC7 And Coiled-Coil Domain-Containing Protein 1, Pleckstrin Homology, Sec7 And Coiled-Coil Domains 1, SEC7 Homolog B2-1, PSCD1, SEC7, Homolog Of Secretory Protein SEC7, Cytoadhesin 1, CYTOHESIN-1, B2-1, Cytohesin-1.
Product # :
PRO-2215Price :
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Shipped with Ice Packs
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Description
CYTH1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 421 amino acids (1-398 a.a) and having a molecular mass of 48.8kDa. CYTH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CYTH1 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Cytohesin 1 also known as CYTH1 belongs to the PSCD family. CYTH1 is responsible for promoting guanine-nucleotide exchange on ARF1 and ARF5 and also promotes the activation of ARF factors by the replacement of GDP with GTP.
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Synonyms
Cytohesin 1, D17S811E, PH, SEC7 And Coiled-Coil Domain-Containing Protein 1, Pleckstrin Homology, Sec7 And Coiled-Coil Domains 1, SEC7 Homolog B2-1, PSCD1, SEC7, Homolog Of Secretory Protein SEC7, Cytoadhesin 1, CYTOHESIN-1, B2-1, Cytohesin-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 MGSMEEDDSY VPSDLTAEER QELENIRRRK QELLADIQRL KDEIAEVANE IENLGSTEER KNMQRNKQVA MGRKKFNMDP KKGIQFLIEN DLLKNTCEDI AQFLYKGEGL NKTAIGDYLG ERDEFNIQVL HAFVELHEFT DLNLVQALRQ FLWSFRLPGE AQKIDRMMEA FAQRYCQCNN GVFQSTDTCY VLSFAIIMLN TSLHNPNVKD KPTVERFIAM NRGINDGGDL PEELLRNLYE SIKNEPFKIP EDDGNDLTHT FFNPDREGWL LKLGGGRVKT WKRRWFILTD NCLYYFEYTT DKEPRGIIPL ENLSIREVED SKKPNCFELY IPDNKDQVIK ACKTEADGRV VEGNHTVYRI SAPTPEEKEE WIKCIKAAIS RDPFYEMLAA RKKKVSSTKR H.
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 :
OSGEP HumanDescription:
O-Sialoglycoprotein Endopeptidase Human Recombinant
O-Sialoglycoprotein Endopeptidase, T(6)A37 Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, TRNA Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, N6-L-Threonylcarbamoyladenine Synthase, T(6)A Synthase, HOSGEP, GCPL1, Probable TRNA Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, Probable TRNA N6-Adenosine Threonylcarbamoyltransferase , Probable O-Sialoglycoprotein Endopeptidase, EC 3.4.24.57, EC 2.3.1.234, FLJ20411, OSGEP1, PRSMG1, KAE1, Probable tRNA N6-adenosine threonylcarbamoyltransferase.
Product # :
ENZ-821Price :
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Description
OSGEP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (1-335 a.a) and having a molecular mass of 38.8kDa. OSGEP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
OSGEP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
O-Sialoglycoprotein Endopeptidase, also known as OSGEP is a member of the KAE1 / TsaD family. OSGEP is essential for the formation of threonylcarbamoyl group on adenosine at position 37 (t6A37) in tRNAs which read codons beginning with adenine. OSGEP take a direct catalytic part in the above reaction, however other proteins of the complex are required to fulfill this activity.
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Synonyms
O-Sialoglycoprotein Endopeptidase, T(6)A37 Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, TRNA Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, N6-L-Threonylcarbamoyladenine Synthase, T(6)A Synthase, HOSGEP, GCPL1, Probable TRNA Threonylcarbamoyladenosine Biosynthesis Protein OSGEP, Probable TRNA N6-Adenosine Threonylcarbamoyltransferase , Probable O-Sialoglycoprotein Endopeptidase, EC 3.4.24.57, EC 2.3.1.234, FLJ20411, OSGEP1, PRSMG1, KAE1, Probable tRNA N6-adenosine threonylcarbamoyltransferase.
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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 MGSMPAVLGF EGSANKIGVG VVRDGKVLAN PRRTYVTPPG TGFLPGDTAR HHRAVILDLL QEALTESGLT SQDIDCIAYT KGPGMGAPLV SVAVVARTVA QLWNKPLVGV NHCIGHIEMG RLITGATSPT VLYVSGGNTQ VIAYSEHRYR IFGETIDIAV GNCLDRFARV LKISNDPSPG YNIEQMAKRG KKLVELPYTV KGMDVSFSGI LSFIEDVAHR MLATGECTPE DLCFSLQETV FAMLVEITER AMAHCGSQEA LIVGGVGCNV RLQEMMATMC QERGARLFAT DERFCIDNGA MIAQAGWEMF RAGHRTPLSD SGVTQRYRTD EVEVTWRD.
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 :
CCL28 HumanDescription:
Mucosae-Associated Epithelial Chemokine Human Recombinant (CCL28)
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
Product # :
CHM-353Price :
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Shipping Method :
Shipped at Room temp
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Description
CCL28 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 108 amino acids and having a molecular mass of 12.3 kDa. The CCL28 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM PBS and 150mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.More Info
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Introduction
CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues. -
Synonyms
MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CCL28 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL28 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 CCL28 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
SEAILPIASS CCTEVSHHIS RRLLERVNMC RIQRADGDCD LAAVILHVKR RRICVSPHNH TVKQWMKVQA AKKNGKGNVC HRKKHHGKRN SNRAHQGKHE TYGHKTPY.
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Background
What is the molecular weight/Mw of CCL28 HUMAN Protein?
CCL28 HUMAN Protein has a total Mw of 12.3kDa.
What is the source or expression system of CCL28 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL28 HUMAN Protein?
CCL28 HUMAN Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL28 HUMAN Protein?
Determined by its ability to chemoattract human lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of CCL28 HUMAN Protein?
SEAILPIASS CCTEVSHHIS RRLLERVNMC RIQRADGDCD LAAVILHVKR RRICVSPHNH TVKQWMKVQA AKKNGKGNVC HRKKHHGKRN SNRAHQGKHE TYGHKTPY.
What applications can CCL28 HUMAN Protein be used in?
CCL28 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL28 HUMAN Protein?
The endotoxin level is minimal, CCL28 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.
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Name :
CX3CL1 RatDescription:
Fractalkine Rat Recombinant (CX3CL1)
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
Product # :
CHM-005Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Fractalkine Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 76 amino acids and having a molecular mass of 8.7kDa.The Fractalkine is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
Determined by its ability to chemoattract human monocytes using a concentration range of 5.0-10.0 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.More Info
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Introduction
Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.
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Synonyms
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized FractalkineRat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fractalkine 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 Fractalkine 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
QHLGMTKCNI TCHKMTSPIP VTLLIHYQLN QESCGKRAII LETRQHRHFC ADPKEKWVQD AMKHLDHQTA ALTRNG
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Background
What is the molecular weight/Mw of CX3CL1 RAT Protein?
CX3CL1 RAT Protein has a total Mw of 8.7kDa.
What is the source or expression system of CX3CL1 RAT Protein?
Escherichia Coli.
What is the Purity of CX3CL1 RAT Protein?
CX3CL1 RAT Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CX3CL1 RAT Protein?
Determined by its ability to chemoattract human monocytes using a concentration range of 5.0-10.0 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.
What is the amino acid sequence of CX3CL1 RAT Protein?
QHLGMTKCNI TCHKMTSPIP VTLLIHYQLN QESCGKRAII LETRQHRHFC ADPKEKWVQD AMKHLDHQTA ALTRNG
What applications can CX3CL1 RAT Protein be used in?
CX3CL1 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CX3CL1 RAT Protein?
The endotoxin level is minimal, CX3CL1 RAT 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 :
TXN1 Human, HisDescription:
Thioredoxin Human Recombinant, His Tag
Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.
Product # :
PRO-804Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Thioredoxin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids (1-105 a.a.) and having a molecular mass of 13.9 kDa (Molecular weight on SDS-PAGE will appear higher). TXN protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
TXN1 solution containing 1x PBS pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is 7-10 A650/min/mg, obtained by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin.More Info
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Introduction
Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation.
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Synonyms
Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.
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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 MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD DCQDVASECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT INELV.
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 :
UMPS HumanDescription:
Uridine Monophosphate Synthetase Human Recombinant
OPRT, Uridine 5'-monophosphate synthase, UMP synthase, Orotate phosphoribosyltransferase , OPRT, OPRTase, Orotidine 5'-phosphate decarboxylase , ODC, OMPdecase.
Product # :
ENZ-663Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
UMPS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 500 amino acids (1-480 a.a) and having a molecular mass of 54.3kDa.UMPS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The UMPS solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Uridine 5'-monophosphate synthase (UMPS), is a bifunctional enzyme that catalyzes the ultimate two steps of the de novo pyrimidine biosynthetic pathway. UMPS in eukaryotes links the orotate phosphoribosyltransferase and the orotidine-5’-monophosphate (OMP) decarboxylase activities into a single protein. The harmony of these 2 enzymes is assumed to be stabilized the catalytic centers as a result of the low molar concentration of the protein in mammalian cells.mutations in this gene are the reason of inherited orotic aciduria disease.
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Synonyms
OPRT, Uridine 5'-monophosphate synthase, UMP synthase, Orotate phosphoribosyltransferase , OPRT, OPRTase, Orotidine 5'-phosphate decarboxylase , ODC, OMPdecase.
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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 MAVARAALGP LVTGLYDVQA FKFGDFVLKS GLSSPIYIDL RGIVSRPRLL SQVADILFQT AQNAGISFDT VCGVPYTALP LATVICSTNQ IPMLIRRKET KDYGTKRLVE GTINPGETCL IIEDVVTSGS SVLETVEVLQ KEGLKVTDAI VLLDREQGGK DKLQAHGIRL HSVCTLSKML EILEQQKKVD AETVGRVKRF IQENVFVAAN HNGSPLSIKE APKELSFGAR AELPRIHPVA SKLLRLMQKK ETNLCLSADV SLARELLQLA DALGPSICML KTHVDILNDF TLDVMKELIT LAKCHEFLIF EDRKFADIGN TVKKQYEGGI FKIASWADLV NAHVVPGSGV VKGLQEVGLP LHRGCLLIAE MSSTGSLATG DYTRAAVRMA EEHSEFVVGF ISGSRVSMKP EFLHLTPGVQ LEAGGDNLGQ QYNSPQEVIG KRGSDIIIVG RGIISAADRL EAAEMYRKAA WEAYLSRLGV.
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 :
CLTA HumanDescription:
Clathrin, Light Chain A Human Recombinant
Clathrin light chain A, Lca, CLTA.
Product # :
PRO-1144Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CLTA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 242 amino acids (1-218 a.a) and having a molecular mass of 26.2kDa (Molecular weight on SDS-PAGE will appear higher).CLTA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CLTA protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Clathrin, light chain A (CLTA) is a member of the clathrin family. Clathrin, which is a large, soluble protein, is comprised of heavy and light chains. CLTA is one of 2 clathrin light chain proteins which are supposed to function as regulatory elements. CLTA is a key cytosolic coat protein in pits and vesicles originating from the plasma membrane and the trans-Golgi network. In receptor-mediated endocytosis, receptor proteins are encapsulated by Clathrin-coated vesicles.
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Synonyms
Clathrin light chain A, Lca, CLTA.
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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 MGSHMAELDP FGAPAGAPGG PALGNGVAGA GEEDPAAAFL AQQESEIAGI ENDEAFAILD GGAPGPQPHG EPPGGPDAVD GVMNGEYYQE SNGPTDSYAA ISQVDRLQSE PESIRKWREE QMERLEALDA NSRKQEAEWK EKAIKELEEW YARQDEQLQK
TKANNRAAEE AFVNDIDESS PGTEWERVAR LCDFNPKSSK QAKDVSRMRS VLISLKQAPL VH.
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 :
CPE HumanDescription:
Carboxypeptidase-E Human Recombinant
Carboxypeptidase E, Carboxypeptidase H, CPH, CPE, CPE Human, Enkephalin convertase, Prohormone-processing carboxypeptidase.
Product # :
ENZ-687Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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Description
CPE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 457 amino acids (43-476 a.a.) and having a molecular mass of 51.4kDa. CPE is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CPE protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Carboxypeptidase-E (CPE ) is a carboxypeptidase that cleaves C-terminal amino acid residues and is involved in the biosynthesis of peptide hormones and neurotransmitters. CPE is a peripheral membrane protein. CPE specifically connects regulated secretory pathway proteins, including prohormones, but constitutively secreted proteins. Mutations in CPE are implicated in type II diabetes.
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Synonyms
Carboxypeptidase E, Carboxypeptidase H, CPH, CPE, CPE Human, Enkephalin convertase, Prohormone-processing carboxypeptidase.
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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 MGSLQQEDGI SFEYHRYPEL REALVSVWLQ CTAISRIYTV GRSFEGRELL VIELSDNPGV HEPGEPEFKY IGNMHGNEAV GRELLIFLAQ YLCNEYQKGN ETIVNLIHST RIHIMPSLNP DGFEKAASQP GELKDWFVGR SNAQGIDLNR NFPDLDRIVY VNEKEGGPNN HLLKNMKKIV DQNTKLAPET KAVIHWIMDI PFVLSANLHG GDLVANYPYD ETRSGSAHEY SSSPDDAIFQ SLARAYSSFN PAMSDPNRPP CRKNDDDSSF VDGTTNGGAW YSVPGGMQDF NYLSSNCFEI TVELSCEKFP PEETLKTYWE DNKNSLISYL EQIHRGVKGF VRDLQGNPIA NATISVEGID HDVTSAKDGD YWRLLIPGNY KLTASAPGYL AITKKVAVPY SPAAGVDFEL ESFSERKEEE KEELMEWWKM MSETLNF.
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 :
P Selectin HumanDescription:
P-selectin Human Recombinant
P-selectin, Granule membrane protein 140, GMP-140, PADGEM, Leukocyte-endothelial cell adhesion molecule 3, LECAM3, CD62 antigen-like family member P, CD62P antigen, SELP, GMRP, GRMP, CD62, PSEL, CD62P, GMP140, FLJ45155.
Product # :
PRO-382Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
P-Selectin Human Recombinant is expressed in E. coli containing 566 amino acids 197-761 fused to an amino terminal hexahistidine tag.
Source
Escherichia Coli.
Formulation
P-Selectin is supplied in 50% Glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Single band on Western Blot.More Info
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Introduction
P-Selectin also called Platelet Alpha-Granule Membrane Protein, CD62, and Granulocyte Membrane Protein GRMP belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. Pselectin is expressed transiently on the surface of activated platelets and endothelial cells. P-Selectin is a 140 kDa protein which is stored in the alpha-granules of platelets and Weibel-Palade bodies of endothelial cells. Secreted P-selectin is thought to play a key role in the adhesion of platelets to monocytes and neutrophils during an inflammatory response. P-Selectin is a calcium-dependent receptor that binds to sialylated forms of Lewis blood group carbohydrate antigens on neutrophils and monocytes. Levels of P-Selectin may be elevated in a number of pathological conditions.
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Synonyms
P-selectin, Granule membrane protein 140, GMP-140, PADGEM, Leukocyte-endothelial cell adhesion molecule 3, LECAM3, CD62 antigen-like family member P, CD62P antigen, SELP, GMRP, GRMP, CD62, PSEL, CD62P, GMP140, FLJ45155.
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Physical Appearance
Sterile Filtered liquid formulation.
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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.
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Applications
P-Selectin 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.
- View Data Sheet
Name :
EPO MouseDescription:
Erythropoietin Mouse Recombinant
Erythropoietin, erythropoietin isoform 1 precursor, Epo.
Product # :
CYT-1171Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
EPO Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 176 amino acids (27-192 aa) and having a molecular mass of 19.8kDa.EPO is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
EPO Mouse protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 2ng/ml.
sds-page
More Info
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Introduction
Erythropoietin or EPO is a hormone (glycoprotein), part of the type I cytokine group of proteins. EPO is found mainly in the kidney tissue, produced from fibroblast-like cortical interstitial cells near the proximal tubules. EPO is also present in the blood, where it acts as red cell production regulator, by the promotion of differentiation of erythroid and thereby starts hemoglobin synthesis. Furthermore, EPO has neuroprotective activity towards brain injuries & anti-apoptotic activity in different tissues.
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Synonyms
Erythropoietin, erythropoietin isoform 1 precursor, Epo.
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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
ADPMAPPRLI CDSRVLERYI LEAKEAENVT MGCAEGPRLS ENITVPDTKV NFYAWKRMEV EEQAIEVWQG LSLLSEAILQ AQALLANSSQ PPETLQLHID KAISGLRSLT SLLRVLGAQK ELMSPPDTTP PAPLRTLTVD TFCKLFRVYA NFLRGKLKLY TGEVCRRGDR HHHHHH.
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Background
What is the molecular weight/Mw of EPO Protein?
EPO Protein has a total Mw of 19.8kDa.
What is the source or expression system of EPO Protein?
Sf9, Baculovirus cells.
What is the Purity of EPO Protein?
EPO Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of EPO Protein?
Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 2ng/ml.
What is the amino acid sequence of EPO Protein?
ADPMAPPRLI CDSRVLERYI LEAKEAENVT MGCAEGPRLS ENITVPDTKV NFYAWKRMEV EEQAIEVWQG LSLLSEAILQ AQALLANSSQ PPETLQLHID KAISGLRSLT SLLRVLGAQK ELMSPPDTTP PAPLRTLTVD TFCKLFRVYA NFLRGKLKLY TGEVCRRGDR HHHHHH.
What applications can EPO Protein be used in?
EPO Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EPO Protein?
The endotoxin level is minimal, EPO 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 :
CCL14 Human (66 a.a.)Description:
HCC-1 Human Recombinant (CCL14) (66 a.a.)
Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.
Product # :
CHM-006Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
HCC-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 66 amino acids and having a molecular mass of 7.8kDa. The HCC-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CCL14 protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% trehalose.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Biological activity is determined by its ability to chemoattract human monocytes using a concentration range of 5.0-20.0 ng/ml.More Info
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Introduction
Chemokine (C-C motif) ligand 14 (CCL14) is a small cytokine belonging to the CC chemokine family. It is also commonly known as HCC-1. It is produced as a protein precursor that is procesed to generate a mature active protein containing 74 amino acids that and is 46% identical in amino acid composition to CCL3 and CCL4. This chemokine is expressed in various tissues including spleen, bone marrow, liver, muscle, and gut. CCL13 activates monocytes, but does not induce their chemotaxis. Human CCL13 is located on chromosome 17 within a cluster of other chemokines belonging to the CC family.
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Synonyms
Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized HCC1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL14 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 HCC-1 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
GPYHPSECCF TYTTYKIPRQ RIMDYYETNS QCSKPGIVFI TKRGHSVCTN PSDKWVQDYI KDMKEN.
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Background
What is the molecular weight/Mw of CCL14 HUMAN (66 A.A.) Protein?
CCL14 HUMAN (66 A.A.) Protein has a total Mw of 7.8kDa.
What is the source or expression system of CCL14 HUMAN (66 A.A.) Protein?
Escherichia Coli.
What is the Purity of CCL14 HUMAN (66 A.A.) Protein?
CCL14 HUMAN (66 A.A.) Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL14 HUMAN (66 A.A.) Protein?
The Biological activity is determined by its ability to chemoattract human monocytes using a concentration range of 5.0-20.0 ng/ml.
What is the amino acid sequence of CCL14 HUMAN (66 A.A.) Protein?
GPYHPSECCF TYTTYKIPRQ RIMDYYETNS QCSKPGIVFI TKRGHSVCTN PSDKWVQDYI KDMKEN.
What applications can CCL14 HUMAN (66 A.A.) Protein be used in?
CCL14 HUMAN (66 A.A.) Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL14 HUMAN (66 A.A.) Protein?
The endotoxin level is minimal, CCL14 HUMAN (66 A.A.) 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 :
CYTIP HumanDescription:
Cytohesin 1 Interacting Protein Human Recombinant
Cytohesin 1 Interacting Protein, Cytohesin Binder And Regulator, PSCDBP, Pleckstrin Homology, Sec7 And Coiled-Coil Domains, Binding Protein,Pleckstrin Homology Sec7 And Coiled-Coil Domains-Binding Protein, Cytohesin-Associated Scaffolding Protein, Cytohesin Binding Protein HE, Cytohesin-Binding Protein HE, Cbp HE, CASP, CYBR, HE Pleckstrin Homology, Sec7 And Coiled/Coil Domains, Binding Protein, Cytohesin-1 Interacting Protein, Cytohesin-Interacting Protein, CYTHIP, B3-1, CYTIP.
Product # :
PRO-2172Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CYTIP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 384 amino acids (1-359 a.a) and having a molecular mass of 42.6kDa.CYTIP is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CYTIP protein solution (1mg/ml) containing 20mM Tris-HCl (pH 8.0) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Cytohesin-interacting protein, also known as CYTIP contains 2 leucine zipper domains as well as a putative C-terminal nuclear targeting signal. However, CYTIP does not contain any hydrophobic regions. In addition, CYTIP is expressed weakly in resting NK and T cells. It also modulates the activation of ARF genes by CYTH1.
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Synonyms
Cytohesin 1 Interacting Protein, Cytohesin Binder And Regulator, PSCDBP, Pleckstrin Homology, Sec7 And Coiled-Coil Domains, Binding Protein,Pleckstrin Homology Sec7 And Coiled-Coil Domains-Binding Protein, Cytohesin-Associated Scaffolding Protein, Cytohesin Binding Protein HE, Cytohesin-Binding Protein HE, Cbp HE, CASP, CYBR, HE Pleckstrin Homology, Sec7 And Coiled/Coil Domains, Binding Protein, Cytohesin-1 Interacting Protein, Cytohesin-Interacting Protein, CYTHIP, B3-1, CYTIP.
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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 SSGLVPPGSH MGSEFMSLQR LLQHSSNGNL ADFCAGPAYS SYSTLTGSLT MDDNRRIQML ADTVATLPRG RKQLALTRSS SLSDFSWSQR KLVTVEKQDN ETFGFEIQSY RPQNQNACSS EMFTLICKIQ EDSPAHCAGL QAGDVLANIN GVSTEGFTYK QVVDLIRSSG NLLTIETLNG TMILKRTELE AKLQVLKQTL KQKWVEYRSL QLQEHRLLHG DAANCPSLEN MDLDELSLFG PLPGPGPALV DRNRLSSESS CKSWLSSMTM DSEDGYQTCV SEDSSRGAFS RQTSTDDECF IPKEGDDFLR RSSSRRNRSI SNTSSGSMSP LWEGNLSSMF GTLPRKSRKG SVRKQLLKFI PGLHRAVEEE ESRF
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 :
Stratifin HumanDescription:
Tyr-3/Trp- 5 Monooxygenase Activation Protein Sigma Human Recombinant
14-3-3 protein sigma, Epithelial cell marker protein 1, HME1, Stratifin, YWHAS, SFN, Stratifin.
Product # :
PKA-357Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Stratifin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 248 amino acids (1-248) and having a molecular mass of 27.7 kDa. Stratifin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Stratifin solution containing 20mM Tris-HCl pH-8, 50mM NaCl and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Stratifin is part of the 14-3-3 family. The 14-3-3 family of proteins plays an important regulatory function in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are 7 isoforms, beta, gamma, epsilon, sigma, zeta, tau and eta that have been identified in mammals. Stratifin is an epithelial cell marker that functions as a tumor suppressor whose expression can be down regulated via methylation. Failure of Stratifin expression results in a defective G2/M phase checkpoint and results in epithelial and non-epithelial tumorigenesis.
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Synonyms
14-3-3 protein sigma, Epithelial cell marker protein 1, HME1, Stratifin, YWHAS, SFN, Stratifin.
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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
MERASLIQKA KLAEQAERYE DMAAFMKGAV EKGEELSCEE RNLLSVAYKN VVGGQRAAWR VLSSIEQKSN EEGSEEKGPE VREYREKVET ELQGVCDTVL GLLDSHLIKE AGDAESRVFY LKMKGDYYRY LAEVATGDDK KRIIDSARSA YQEAMDISKK EMPPTNPIRL GLALNFSVFH YEIANSPEEA ISLAKTTFDE AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADNAGEEGG EAPQEPQS.
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 :
CXCL14 RatDescription:
BRAK (CXCL14) Rat Recombinant
C-X-C motif chemokine 14, B-cell and monocyte-activating chemokine, Chemokine BRAK, Kidney-expressed chemokine CXC, MIP-2G, Small-inducible cytokine B14, Cxcl14, Bmac, Kec, Ks1, Mip2g, Scyb14, BRAK, NJAC, AI414372, bolekine, MIP2gamma, 1110031L23Rik, 1200006I23Rik.
Product # :
CHM-021Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
CXCL14 Rat Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 77 amino acids and having a molecular mass of 9.4kDa.The CXCL14 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CXCL14 was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract activated monocytes using a concentration range of 1.0-10.0 ng/ml.More Info
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Introduction
CXCL14 is involved in immunoregulatory and inflammatory processes. BRAK protein is structurally related to the CXC (Cys-X-Cys) subfamily of cytokines. CXCL14 displays chemotactic activity for monocytes but not for lymphocytes, dendritic cells, neutrophils or macrophages. CXCL14 is involved in the homeostasis of monocyte-derived macrophages.
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Synonyms
C-X-C motif chemokine 14, B-cell and monocyte-activating chemokine, Chemokine BRAK, Kidney-expressed chemokine CXC, MIP-2G, Small-inducible cytokine B14, Cxcl14, Bmac, Kec, Ks1, Mip2g, Scyb14, BRAK, NJAC, AI414372, bolekine, MIP2gamma, 1110031L23Rik, 1200006I23Rik.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CXCL14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL14 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 CXCL14 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
SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIITTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.
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Background
What is the molecular weight/Mw of CXCL14 RAT Protein?
CXCL14 RAT Protein has a total Mw of 9.4kDa.
What is the source or expression system of CXCL14 RAT Protein?
Escherichia Coli.
What is the Purity of CXCL14 RAT Protein?
CXCL14 RAT Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL14 RAT Protein?
Determined by its ability to chemoattract activated monocytes using a concentration range of 1.0-10.0 ng/ml.
What is the amino acid sequence of CXCL14 RAT Protein?
SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIITTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.
What applications can CXCL14 RAT Protein be used in?
CXCL14 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL14 RAT Protein?
The endotoxin level is minimal, CXCL14 RAT 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 :
GCHFR HumanDescription:
GTP Cyclohydrolase I Feedback Regulator Human Recombinant
GFRP, HsT16933, P35,GTP cyclohydrolase 1 feedback regulatory protein, GTP cyclohydrolase I feedback regulatory protein, p35, GCHFR
Product # :
PRO-2006Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GCHFR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 107 amino acids (1-84a.a) and having a molecular mass of 12.1kDa. GCHFR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GCHFR protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 40% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
GTP Cyclohydrolase I Feedback Regulator, also known as GCHFR, is a Protein coding gene which includes a homodimer. GCHFR binds and mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase I. GCHFR also regulates phenylalanine metabolism in the liver and in the production of biogenic amine neurotransmitters and nitric oxide.
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Synonyms
GFRP, HsT16933, P35,GTP cyclohydrolase 1 feedback regulatory protein, GTP cyclohydrolase I feedback regulatory protein, p35, GCHFR
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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 MGSMPYLLIS TQIRMEVGPT MVGDEQSDPE LMQHLGASKR RALGNNFYEY YVDDPPRIVL DKLERRGFRV LSMTGVGQTL VWCLHKE.
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 :
GNLY HumanDescription:
Granulysin Human Recombinant
LAG2, Lymphokine LAG-2, TLA519, NKG5, LAG2, D2S69E, Granulysin, T-cell activation protein 519, GNLY, D2S69E.
Product # :
PRO-852Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GNLY Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 159 amino acids and fused to a double His Tag (N+C terminus) and having a total molecular mass of 18.1 kDa.The GNLY is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Granulysin protein was lyophilized from a concentrated (1mg/ml) solution containing no additives.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
GNLY is part of the SAPLIP family and is located in the cytotoxic granules of T cells, which are discharged upon antigen stimulation. GNLY is localized in cytotoxic granules of cytotoxic T lymphocytes and natural killer cells, and it has antimicrobial activity against M. tuberculosis and other organisms. GNLY is an antimicrobial protein that kills intracellular pathogens. GNLY is active against a wide range of microbes, including Gram-positive and Gram-negative bacteria, fungi, and parasites. Kills Mycobacterium tuberculosis.
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Synonyms
LAG2, Lymphokine LAG-2, TLA519, NKG5, LAG2, D2S69E, Granulysin, T-cell activation protein 519, GNLY, D2S69E.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Granulysin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Granulysin 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 Granulysin 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
MGSSHHHHHHSSGLVPRGSHMMEGLVFSRLSPEYYD
LARAHLRDEEKSCPCLAQEGPQGDLLTKTQELGRDYR
TCLTIVQKLKKMVDKPTQRSVSNAATRVCRTGRSRWR
DVCRNFMRRYQSRVTQGLVAGETAQQICEDLRLCIPS
TGPLGSHHHHHH.
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 :
GDF6 HumanDescription:
Bone Morphogenetic protein-13 Human Recombinant
Growth Differentiation Factor 6, Growth/Differentiation Factor 16, Bone Morphogenetic Protein 13, BMP-13, BMP13, GDF-6, Klippel-Feil Malformation, Segmentation Syndrome 1, Klip-Feil Malformation, Klippel-Feil Syndrome, MCOPCB6, SCDO4, CDMP2, LCA17, MCOP4, GDF16, KFS1, KFSL, SGM1, KFM, KFS, GDF6.
Product # :
CYT-938Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
BMP13 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 120 amino acids and having a molecular mass of 27.1kDa.The BMP-13 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BMP-13 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.
Purity
Greater than 95.0% as determined by: (a) Analysis by HPLC. (b) Analysis by SDS-PAGE.
Biological Activity
The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 2.0µg/ml, corresponding to a specific activity of > 500IU/mg.More Info
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Introduction
Growth/differentiation factors (GDF1-GDF15) belong to the BMP family of TGF-beta superfamily proteins. These factors are produced as inactive preproproteins which are subsequently cleaved and assembled into active secreted homodimers. BMP13 is a growth factor which controls proliferation and cellular differentiation in the retina and bone formation. BMP13 has a central role in regulating apoptosis during retinal development. GDF proteins are vital during embryonic development, particularly in the skeletal, nervous, and muscular systems. BMP13 gene mutations result in colobomata, which are congenital abnormalities in ocular development, and in Klippel-Feil syndrome (KFS), which is a congenital disorder of spinal segmentation.
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Synonyms
Growth Differentiation Factor 6, Growth/Differentiation Factor 16, Bone Morphogenetic Protein 13, BMP-13, BMP13, GDF-6, Klippel-Feil Malformation, Segmentation Syndrome 1, Klip-Feil Malformation, Klippel-Feil Syndrome, MCOPCB6, SCDO4, CDMP2, LCA17, MCOP4, GDF16, KFS1, KFSL, SGM1, KFM, KFS, GDF6.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BMP13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-13 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 BMP13 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
TAFASRHGKR HGKKSRLRCS KKPLHVNFKE LGWDDWIIAP LEYEAYHCEG VCDFPLRSHL EPTNHAIIQT LMNSMDPGST PPSCCVPTKL TPISILYIDA GNNVVYKQYE DMVVESCGCR.
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Background
Bone Morphogenetic Protein-13 Human Recombinant: Unraveling its Potential in Tissue Engineering and Regenerative Medicine
Abstract:
Bone Morphogenetic Protein-13 (BMP-13) human recombinant is a pivotal member of the bone morphogenetic protein family, known for its crucial role in tissue development, regeneration, and repair. This research paper aims to provide a comprehensive analysis of BMP-13, including its characteristics, signaling pathways, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of BMP-13 human recombinant are proposed, shedding light on its future implications in the field of tissue engineering and regenerative medicine.
Introduction:
Tissue engineering and regenerative medicine hold great promise in addressing tissue repair and regeneration challenges. BMP-13, a prominent member of the BMP family, plays a vital role in orchestrating cellular responses during tissue development and healing. This paper explores the distinctive features of BMP-13 and presents novel approaches for the production and optimization of BMP-13 human recombinant, aiming to unlock its therapeutic potential in various regenerative contexts.
Characteristics and Signaling Pathways:
BMP-13 is a secreted growth factor belonging to the transforming growth factor-beta (TGF-β) superfamily. It exerts its biological effects by binding to specific cell surface receptors, initiating intricate intracellular signaling cascades. BMP-13 signaling pathways, including Smad-dependent and Smad-independent pathways, regulate critical processes such as cell differentiation, proliferation, and extracellular matrix synthesis, influencing tissue development and repair.
Production of BMP-13 Human Recombinant:
Efficient production methodologies are crucial for harnessing the therapeutic potential of BMP-13 human recombinant. Various recombinant protein expression systems, such as mammalian cells or baculovirus-insect cell systems, have been utilized for the production of functional BMP-13. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding enhancement, have been employed to improve the yield and bioactivity of BMP-13 recombinant protein.
Potential Therapeutic Applications:
BMP-13 human recombinant holds immense promise in the field of tissue engineering and regenerative medicine. Its involvement in cartilage formation, osteogenesis, and tissue repair makes it a potential candidate for the treatment of musculoskeletal disorders, joint injuries, and cartilage defects. Furthermore, the ability of BMP-13 to modulate cell behavior and tissue remodeling indicates its wider therapeutic applications in diverse regenerative processes.
Conclusion:
BMP-13 human recombinant emerges as a crucial regulator in tissue engineering and regenerative medicine, offering significant potential for tissue repair and regeneration. Optimizing production methodologies and further unraveling its signaling mechanisms will undoubtedly enhance its therapeutic applications. Given its involvement in cartilage and bone formation, as well as tissue repair, BMP-13 human recombinant represents a valuable tool for promoting tissue regeneration and addressing the unmet clinical needs in regenerative medicine.
What is the molecular weight/Mw of GDF6 Protein?
GDF6 Protein has a total Mw of 27.1kDa.
What is the source or expression system of GDF6 Protein?
Escherichia Coli.
What is the Purity of GDF6 Protein?
GDF6 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF6 Protein?
The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 2.0µg/ml, corresponding to a specific activity of > 500IU/mg.
What is the amino acid sequence of GDF6 Protein?
TAFASRHGKR HGKKSRLRCS KKPLHVNFKE LGWDDWIIAP LEYEAYHCEG VCDFPLRSHL EPTNHAIIQT LMNSMDPGST PPSCCVPTKL TPISILYIDA GNNVVYKQYE DMVVESCGCR.
What applications can GDF6 Protein be used in?
GDF6 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF6 Protein?
The endotoxin level is minimal, GDF6 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 :
PTMS HumanDescription:
Prothymosin Human Recombinant
ParaT, parathymosin.
Product # :
PRO-1735Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PTMS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 125 amino acids (1-102aa) and having a molecular mass of 13.9kDa.PTMS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PTMS protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Parathymosin, also known as PTMS is a member of the pro/parathymosin family. PTMS may mediate immune function by blocking the effect of prothymosin alpha which confers resistance to particular opportunistic infections. Among the diseases associated with PTMS are hepatitis b, and alzheimer's disease.
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Synonyms
ParaT, parathymosin.
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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 MGSMSEKSVE AAAELSAKDL KEKKEKVEEK ASRKERKKEV VEEEENGAEE EEEETAEDGE EEDEGEEEDE EEEEEDDEGP ALKRAAEEED EADPKRQKTE NGASA
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 :
CTF1 RatDescription:
Cardiotrophin-1 Rat Recombinant
Cardiotrophin-1, CT-1, Ctf1.
Product # :
CYT-199Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
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- purity
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Description
Cardiotrophin-1 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 203 amino acids and having a molecular mass of 21.4kDa.The CTF1 Rat is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.
Biological Activity
The ED50 as determined by the dose-dependent proliferation of TF-1 cells was found to be < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.More Info
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Introduction
Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction. -
Synonyms
Cardiotrophin-1, CT-1, Ctf1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Cardiotrophin-1 Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTF1 Rat 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 CTF1 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MSQREGSLED HQTDSSFSFL PHLEAKIRQT HNLARLLTKY ADQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSALPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP VPEPVATSAL FTSNSAAGVF SAKVLGLHVC GLYGEWVSRT EGDLGQLVPG GVA.
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Background
What is the molecular weight/Mw of CTF1 Protein?
CTF1 Protein has a total Mw of 21.4kDa.
What is the source or expression system of CTF1 Protein?
Escherichia Coli.
What is the Purity of CTF1 Protein?
CTF1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CTF1 Protein?
The ED50 as determined by the dose-dependent proliferation of TF-1 cells was found to be < 0.5ng/ml, corresponding to a specific activity of > 2.0×106 units/mg.
What is the amino acid sequence of CTF1 Protein?
MSQREGSLED HQTDSSFSFL PHLEAKIRQT HNLARLLTKY ADQLLEEYVQ QQGEPFGLPG FSPPRLPLAG LSGPAPSHAG LPVSERLRQD AAALSALPAL LDAVRRRQAE LNPRAPRLLR SLEDAARQVR ALGAAVETVL AALGAAARGP VPEPVATSAL FTSNSAAGVF SAKVLGLHVC GLYGEWVSRT EGDLGQLVPG GVA.
What applications can CTF1 Protein be used in?
CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CTF1 Protein?
The endotoxin level is minimal, CTF1 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 :
CTSZ MouseDescription:
Cathepsin-Z Mouse Recombinant
Cathepsin Z, CTSZ.
Product # :
ENZ-934Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CTSZ produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 292 amino acids (23-306a.a.) and having a molecular mass of 32.8kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). CTSZ is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CTSZ protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and member of the peptidase C1 family. CTSZ, which has been also known as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and, similar to other members of this family, takes part in tumorigenesis.
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Synonyms
Cathepsin Z, CTSZ.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
ARARLYFRSG QTCYHPIRGD QLALLGRRTY PRPHEYLSPA DLPKNWDWRN VNGVNYASVT RNQHIPQYCG SCWAHGSTSA MADRINIKRK GAWPSILLSV QNVIDCGNAG SCEGGNDLPV WEYAHKHGIP DETCNNYQAK DQDCDKFNQC GTCTEFKECH TIQNYTLWRV GDYGSLSGRE KMMAEIYANG PISCGIMATE MMSNYTGGIY AEHQDQAVIN HIISVAGWGV SNDGIEYWIV RNSWGEPWGE KGWMRIVTST YKGGTGDSYN LAIESACTFG DPIVLEHHHH HH.
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 :
Eotaxin RatDescription:
Eotaxin Rat Recombinant (CCL11)
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11.
Product # :
CHM-260Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- source
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- purity
- biological activity
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Description
Eotaxin Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids and having a molecular mass of 8.4kDa. The CCL11 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in in 1×PBS, pH7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract purified blood eosinophils using a concentration range of 0.1-1.0 ug/ml, corresponding to a Specific Activity of 10-100IU/mg.More Info
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Introduction
Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.
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Synonyms
Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Eotaxin although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution CCL11 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 Eotaxin 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
HPGSIPTSCC FTMTSKKIPN TLLKSYKRIT NNRCTLKAIV FKTKLGKEICADPKKKWVQD ATKHLDQKLQ TPKP.
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Background
What is the molecular weight/Mw of EOTAXIN RAT Protein?
EOTAXIN RAT Protein has a total Mw of 8.4kDa.
What is the source or expression system of EOTAXIN RAT Protein?
Escherichia Coli.
What is the Purity of EOTAXIN RAT Protein?
EOTAXIN RAT Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of EOTAXIN RAT Protein?
Determined by its ability to chemoattract purified blood eosinophils using a concentration range of 0.1-1.0 ug/ml, corresponding to a Specific Activity of 10-100IU/mg.
What is the amino acid sequence of EOTAXIN RAT Protein?
HPGSIPTSCC FTMTSKKIPN TLLKSYKRIT NNRCTLKAIV FKTKLGKEICADPKKKWVQD ATKHLDQKLQ TPKP.
What applications can EOTAXIN RAT Protein be used in?
EOTAXIN RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EOTAXIN RAT Protein?
The endotoxin level is minimal, EOTAXIN RAT 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 :
TECK HumanDescription:
Thymus Expressed Chemokine Human Recombinant (CCL25)
C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.
Product # :
CHM-364Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
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- purity
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Description
TECK Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 14.2kDa. The TECK is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 20mM PB, pH 7.4, 150mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human monocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.More Info
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Introduction
CCL25 (Teck) is a novel CC chemokine, which is distantly related (about 20% amino acid sequence identity) to other CC chemokines. The mouse CCL25 cDNA has also been cloned and shown to encode a 144 a.a. protein, which exhibits 49% a.a. sequence identity to the human CCL25. Human and mouse CCL25 expression was shown to be greatly restricted to the thymus and small intestine. While dendritic cells are identified as the source of CCL25 production in the thymus, dendritic cells derived from bone marrow do not express CCL25. CCL25 signals through the CCR9 receptor. Teck is possibly involved in T-cell development.
Recombinant human and mouse Teck were shown to be chemotactic for activated macrophages, dendritic cells and thymocytes. The recombinant protein demonstrates chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritic cells but is inactive on peripheral blood lymphocytes and neutrophils. -
Synonyms
C-C motif chemokine 25, Small-inducible cytokine A25, Thymus-expressed chemokine, Chemokine TECK, CCL25, SCYA25, TECK, Ckb15, MGC150327.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TECK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TECK 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 TECK 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
QGVFEDCCLA YHYPIGWAVL RRAWTYRIQE VSGSCNLPAA IFYLPKRHRK VCGNPKSREV QRAMKLLDAR NKVFAKLHHN MQTFQAGPHA VKKLSSGNSK LSSSKFSNPI SSSRKNVSLL ISANSGL.
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.