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1000 results found for “tslp”
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Name :
BCL2L1 MouseDescription:
BCL2-Like 1 Recombinant Mouse
Bcl-2-like protein 1, Bcl2-L-1, Apoptosis regulator Bcl-X.
Product # :
PRO-2239Price :
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Shipped with Ice Packs
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Description
BCL2L1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-209 a.a) and having a molecular mass of 25.8kDa. BCL2L1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BCL2L1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
BCL2-Like 1 (BCL2L1) belongs to the BCL-2 protein family. BCL2L1 is found at the outer mitochondrial membrane controls outer mitochondrial membrane channel (VDAC) opening. In addition, BCL2L1 regulate s a switch between cell death modes during mitotic arrest.
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Synonyms
Bcl-2-like protein 1, Bcl2-L-1, Apoptosis regulator Bcl-X.
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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 MGSMSQSNRE LVVDFLSYKL SQKGYSWSQF SDVEENRTEA PEETEAERET PSAINGNPSW HLADSPAVNG ATGHSSSLDA REVIPMAAVK QALREAGDEF ELRYRRAFSD LTSQLHITPG TAYQSFEQVV NELFRDGVNW GRIVAFFSFG GALCVESVDK EMQVLVSRIA SWMATYLNDH LEPWIQENGG WDTFVDLYGN NAAAESRKGQ ER.
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 :
SRSF1 HumanDescription:
Serine/arginine-Rich Splicing Factor 1 Human Recombinant
ASF, MGC5228, SF2, SF2p33, SRp30a, Serine/arginine-rich splicing factor 1, SRSF1, splicing factor 1, ASF-1, Splicing factor, arginine/serine-rich 1, pre-mRNA-splicing factor SF2, P33 subunit, OK/SW-cl.3.
Product # :
PRO-1352Price :
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Description
SRSF1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 268 amino acids (1-248) and having a molecular mass of 29.9 kDa.SRSF1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SRSF1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Serine/arginine-rich splicing factor 1 (SFRS1) belongs to the arginine/serine-rich splicing factor protein family, and functions in both constitutive and alternative pre-mRNA splicing. SFRS1 binds to pre-mRNA transcripts and components of the spliceosome, and can either initiate or inhibit splicing depending on the position of the pre-mRNA binding site. The ability of SFRS1 to activate splicing is controlled by phosphorylation and interactions with other splicing factor associated proteins.
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Synonyms
ASF, MGC5228, SF2, SF2p33, SRp30a, Serine/arginine-rich splicing factor 1, SRSF1, splicing factor 1, ASF-1, Splicing factor, arginine/serine-rich 1, pre-mRNA-splicing factor SF2, P33 subunit, OK/SW-cl.3.
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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 MSGGGVIRGP AGNNDCRIYV GNLPPDIRTK DIEDVFYKYG AIRDIDLKNR RGGPPFAFVE FEDPRDAEDA VYGRDGYDYD GYRLRVEFPR SGRGTGRGGG GGGGGGAPRG RYGPPSRRSE NRVVVSGLPP SGSWQDLKDH MREAGDVCYA DVYRDGTGVV EFVRKEDMTY AVRKLDNTKF RSHEGETAYI RVKVDGPRSP SYGRSRSRSR SRSRSRSRSN SRSRSYSPRR SRGSPRYSPR HSRSRSRT.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
C17ORF103 HumanDescription:
Chromosome 17 Open Reading Frame 103 Human Recombinant
Chromosome 17 Open Reading Frame 103, Transcript Expressed During Hematopoiesis 2, Gene Trap Locus F3b, Gtlf3b, Protein GTLF3B.
Product # :
PRO-1619Price :
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Description
C17ORF103 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 136 amino acids (1-113) and having a molecular mass of 15.4kDa.C17ORF103 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The C17ORF103 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
C17orf103 is a member of the GTLF3B family and is encoded by a gene which is located in human chromosome 17p11.2. BRCA1 and p53 are 2 main tumor suppressor genes which are linked to chromosome 17. Tumor suppressor p53 is necessary for maintenance of cellular genetic integrity by moderating cell fate through DNA repair versus cell death. C17orf103 is also related to neurofibromatosis, a disorder characterized by neural and epidermal lesions, and dysregulated Schwann cell growth.
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Synonyms
Chromosome 17 Open Reading Frame 103, Transcript Expressed During Hematopoiesis 2, Gene Trap Locus F3b, Gtlf3b, Protein GTLF3B.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAHSAAA VPLGALEQGC PIRVEHDRRR RQFTVRLNGC HDRAVLLYEY VGKRIVDLQH TEVPDAYRGR GIAKHLAKAA LDFVVEEDLK AHLTCWYIQK YVKENPLPQY LERLQP
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CCL17 HumanDescription:
Thymus & Activation Regulated Chemokine Human Recombinant (CCL17)
C-C motif chemokine 17, Small-inducible cytokine A17, Thymus and activation-regulated chemokine, CC chemokine TARC, ABCD-2, CCL17, CCL-17, SCYA17, TARC, A-152E5.3, MGC138271, MGC138273.
Product # :
CHM-240Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CCL17 Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 71 amino acids and having a molecular mass of 8 kDa. The TARC is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (0.5mg/ml) solution containing 20mM PBS & 150mM NaCl pH-7.4.
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 human T-Lymphocytes using a concentration range of 1.0-10.0 ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.Citations
More Info
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Introduction
TARC cDNA encodes a 94 amino acid precursor protein with a 23 amino acid residue signal peptide that is cleaved off to generate the 71 amino acid residue mature secreted protein. Along with CC chemokine family members, CCL-17 has approximately 24-29% amino acid sequence identity with RANTES, MIP-1a, MIP-1b, MCP-1, MCP-2, MCP-3 and I-309. TARC is expressed in thymus, and at a lower level in the lung, colon, and small intestine. TARC is in addition transiently expressed in stimulated peripheral blood mononuclear cells. Recombinant TARC has been shown to be chemotactic for T cell lines but not monocytes or neutrophils. CCL-17 was recently identified to be a specific functional ligand for CCR4, a receptor that is selectively expressed on T cells. CCL17 is one of quite a few Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. CCL17 shows chemotactic activity for T lymphocytes, but not monocytes or granulocytes. CCL17 binds to chemokine receptors CCR4 and CCR8. This chemokine plays important roles in T cell development in thymus as well as in trafficking and activation of mature T cells.
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Synonyms
C-C motif chemokine 17, Small-inducible cytokine A17, Thymus and activation-regulated chemokine, CC chemokine TARC, ABCD-2, CCL17, CCL-17, SCYA17, TARC, A-152E5.3, MGC138271, MGC138273.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TARC although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TARC 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 CCL17 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
ARGTNVGRECCLEYFKGAIPLRKLKTWYQTSEDCSRD
AIVFVTVQGRAICSDPNNK RVKNAVKYLQSLERS. -
Background
What is the molecular weight/Mw of CCL17 HUMAN Protein?
CCL17 HUMAN Protein has a total Mw of 8kDa.
What is the source or expression system of CCL17 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL17 HUMAN Protein?
CCL17 HUMAN Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL17 HUMAN Protein?
Determined by its ability to chemoattract human T-Lymphocytes using a concentration range of 1.0-10.0 ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of CCL17 HUMAN Protein?
ARGTNVGRECCLEYFKGAIPLRKLKTWYQTSEDCSRD
AIVFVTVQGRAICSDPNNK RVKNAVKYLQSLERS.
What applications can CCL17 HUMAN Protein be used in?
CCL17 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL17 HUMAN Protein?
The endotoxin level is minimal, CCL17 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL17 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 CCL17 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.
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Name :
CCL25 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 :
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Shipped at Room temp
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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.Citations
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.
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Background
What is the molecular weight/Mw of CCL25 HUMAN Protein?
CCL25 HUMAN Protein has a total Mw of 14.2kDa.
What is the source or expression system of CCL25 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL25 HUMAN Protein?
CCL25 HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL25 HUMAN Protein?
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.
What is the amino acid sequence of CCL25 HUMAN Protein?
QGVFEDCCLA YHYPIGWAVL RRAWTYRIQE VSGSCNLPAA IFYLPKRHRK VCGNPKSREV QRAMKLLDAR NKVFAKLHHN MQTFQAGPHA VKKLSSGNSK LSSSKFSNPI SSSRKNVSLL ISANSGL.
What applications can CCL25 HUMAN Protein be used in?
CCL25 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL25 HUMAN Protein?
The endotoxin level is minimal, CCL25 HUMAN Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL25 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 CCL25 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.
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Name :
TFRC HumanDescription:
Transferrin Receptor Human Recombinant
Transferrin receptor protein 1, TR, TfR, TfR1, Trfr, T9, p90, CD_antigen: CD71, Transferrin receptor, serum form, sTfR, TFRC, CD71.
Product # :
PRO-2180Price :
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Shipped with Ice Packs
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Description
TFRC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 696 amino acids (89-760 a.a) and having a molecular mass of 77.7 kDa.TFRC is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TFRC protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Transferrin receptor protein 1 (TFRC) is required for iron delivery from transferring to cells. The TFRC protein is a transmembrane glycoprotein comprised of 2 disulfide-linked monomers joined by 2 disulfide bonds. Each monomer will bind one holo-transferrin molecule producing an iron-Tf-TfR complex which enters the cell by endocytosis.
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Synonyms
Transferrin receptor protein 1, TR, TfR, TfR1, Trfr, T9, p90, CD_antigen: CD71, Transferrin receptor, serum form, sTfR, TFRC, CD71.
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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 MGSMCKGVEP KTECERLAGT ESPVREEPGE DFPAARRLYW DDLKRKLSEK LDSTDFTGTI KLLNENSYVP REAGSQKDEN LALYVENQFR EFKLSKVWRD QHFVKIQVKD SAQNSVIIVD KNGRLVYLVE NPGGYVAYSK AATVTGKLVH ANFGTKKDFE DLYTPVNGSI VIVRAGKITF AEKVANAESL NAIGVLIYMD QTKFPIVNAE LSFFGHAHLG TGDPYTPGFP SFNHTQFPPS RSSGLPNIPV QTISRAAAEK LFGNMEGDCP SDWKTDSTCR MVTSESKNVK LTVSNVLKEI KILNIFGVIK GFVEPDHYVV VGAQRDAWGP GAAKSGVGTA LLLKLAQMFS DMVLKDGFQP SRSIIFASWS AGDFGSVGAT EWLEGYLSSL HLKAFTYINL DKAVLGTSNF KVSASPLLYT LIEKTMQNVK HPVTGQFLYQ DSNWASKVEK LTLDNAAFPF LAYSGIPAVS FCFCEDTDYP YLGTTMDTYK ELIERIPELN KVARAAAEVA GQFVIKLTHD VELNLDYERY NSQLLSFVRD LNQYRADIKE MGLSLQWLYS ARGDFFRATS RLTTDFGNAE KTDRFVMKKL NDRVMRVEYH FLSPYVSPKE SPFRHVFWGS GSHTLPALLE NLKLRKQNNG AFNETLFRNQ LALATWTIQG AANALSGDVW DIDNEF.
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 :
PLSCR3 HumanDescription:
Phospholipid Scramblase 3 Human Recombinant
Phospholipid scramblase 3, PL scramblase 3, Ca(2+)-dependent phospholipid scramblase 3.
Product # :
PRO-1733Price :
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Description
PLSCR3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids (1-265 a.a) and having a molecular mass of 30.9kDa.PLSCR3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PLSCR3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M urea.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Phospholipid Scramblase 3, (PLSCR3) may mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions which results in a loss of phospholipid asymmetry in the plasma membrane. PLSCR3 may play a key role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system. In addition, PLSCR3 seems to play a role in apoptosis, through translocation of cardiolipin from the inner to the outer mitochondrial membrane which promotes BID recruitment and enhances tBid-induced mitochondrial damages. Among the diseases associated with PLSCR3 are brain ischemia, and ischemia.
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Synonyms
Phospholipid scramblase 3, PL scramblase 3, Ca(2+)-dependent phospholipid scramblase 3.
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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
MGSSHHHHHH SSGLVPRGSH MGSMAGYLPP KGYAPSPPPP YPVTPGYPEP ALHPGPGQAP VPAQVPAPAP GFALFPSPGP VALGSAAPFL PLPGVPSGLE FLVQIDQILI HQKAERVETF LGWETCNRYE LRSGAGQPLG QAAEESNCCA RLCCGARRPL RVRLADPGDR EVLRLLRPLH CGCSCCPCGL QEMEVQAPPG TTIGHVLQTW HPFLPKFSIQ DADRQTVLRV VGPCWTCGCG TDTNFEVKTR DESRSVGRIS KQWGGLVREA LTDADDFGLQ FPLDLDVR
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 :
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 :
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Shipped with Ice Packs
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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.
Citations
More Info
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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.
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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 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 :
Troponin-C ProteinDescription:
Cardiac Troponin-C Human
Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.
Product # :
PRO-2571Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Troponin-C Human produced from Human Cardiac Tissue, having a molecular mass of 18kDa. The Troponin-C is purified using a combination of ion-exchange and affinity chromatography steps.
Source
Human cardiac tissue
Formulation
The protein solution contains 150 mM NaCl, 10 mM sodium phosphate and 0.05% NaN3, (pH 7.0).
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Troponin is a fundamental regulatory protein of striated muscle contraction, and together with tropomyosin, is positioned on the actin filament. Troponin has 3 subunits: TnI- the inhibitor of actomyosin ATPase; TnT- contains the binding site for tropomyosin; and TnC- the protein encoded by the TNNC1 gene. The binding of calcium to TnC stops the inhibitory action of TnI, consequently allowing the interaction of actin with myosin, the hydrolysis of ATP, and the generation of tension. Mutations in the TNNC1 gene are linked to cardiomyopathy dilated type 1Z.
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Synonyms
Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.
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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.
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 :
Leptin tA MouseDescription:
Leptin Antagonist Triple Mutant Mouse Recombinant
Product # :
CYT-354Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Antagonist Triple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, LEP was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
ProSpec’s Leptin Antagonist Triple Mutant Mouse Recombinant is capable of inhibiting Leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human Leptin receptor. It also inhibits various Leptin effects in several in vitro bioassays.Citations
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.201 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
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 :
Leptin tA Mouse, PEG (D23L)Description:
Leptin Triple Antagonist (D23L) Pegylated Mouse Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1242Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Antagonist Triple Mutant D23L Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus. The Leptin antagonist was mutated, resulting in L39A/D40A/F41A mutant. The Mouse Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Mouse Leptin triple anatagonist runs as a 48 kDa. Leptin Antagonist Triple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Mouse Leptin triple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Leptin Antagonist Triple Mutant D23L Mouse Recombinant is capable of stimulating proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is only slightly lower than the non-pegylated recombinant mouse leptin but in vivo it has profound weight reducing effect (as compared to the non-pegylated recombinant mouse leptin), resulting mainly from reduced food intake.
Citations
More Info
-
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
-
Physical Appearance
White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
-
Background
Leptin is a hormone which mainly produced by adipocytes . Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin effects mainly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor is found on a wide range of cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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 :
PSPH HumanDescription:
Phosphoserine Phosphatase Human Recombinant
Phosphoserine phosphatase, EC 3.1.3.3, PSP, O-phosphoserine phosphohydrolase, PSPase, L-3-phosphoserine phosphatase, PSPH.
Product # :
PKA-224Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Phosphoserine Phosphatase Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids and having a molecular mass of 25 kDa. PSP was overexpressed in E. coli and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The protein contains 20mM Hepes pH 7.5, 1mM DTT &100mM KCl2.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
-
Introduction
Human Phosphoserine phosphatase (hPSP) is an important enzyme in the phosphorylated pathway of serine biosynthesis, which contributes a major portion of the endogenous L-serine. Similar to known L-3-phosphoserine phosphatases, it catalyzed the Mg2+-dependent hydrolysis of L-phosphoserine and an exchange reaction between L-serine and L-phosphoserine. Recently, its complex structures reveal that the open-closed environmental change of the active site, generated -helical bundle domain, is important to substrate by local rearrangement of the recognition and hydrolysis.
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Synonyms
Phosphoserine phosphatase, EC 3.1.3.3, PSP, O-phosphoserine phosphohydrolase, PSPase, L-3-phosphoserine phosphatase, PSPH.
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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
MVSHSELRKL FYSADAVCFD VDSTVIREEG IDELAKICGV EDAVSEMTRR AMGGAVPFKA ALTERLALIQ PSREQVQRLI AEQPPHLTPG IRELVSRLQE RNVQVFLISG GFRSIVEHVA SKLNIPATNV FANRLKFYFN GEYAGFDETQ PTAESGGKGK VIKLLKEKFH FKKIIMIGDG ATDMEACPPA DAFIGFGGNV IRQQVKDNAK WYITDFVELL GELEE.
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 :
MAPRE3 HumanDescription:
Microtubule-Associated Protein, RP/EB Family, Member 3 Human Recombinant
RP3, EB3, EBF3, End-binding protein 3, EBF3-S, APC binding protein.
Product # :
PRO-264Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MAPRE3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 301 amino acids (1-281a.a.) and having a molecular mass of 34.1kDa.MAPRE3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MAPRE3 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 2mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
MAPRE3 is a microtubule related protein that cooperates with the colorectal adenomatous polyposis coli tumor suppressor protein and takes a curtail part in regulating microtubule dynamics, cell polarity, and chromosome stability. MAPRE3 protein is related to MAPRE1 and also associates with the microtubule cytoskeleton. MAPRE3 is expressed mainly in the central nervous system and specially associates with APCL, a homolog of the adenomatous polyposis coli tumor suppressor protein.
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Synonyms
RP3, EB3, EBF3, End-binding protein 3, EBF3-S, APC binding protein.
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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.Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAVNVYSTSV TSENLSRHDM LAWVNDSLHL NYTKIEQLCS GAAYCQFMDM LFPGCVHLRK VKFQAKLEHE YIHNFKVLQA AFKKMGVDKI IPVEKLVKGK FQDNFEFIQW FKKFFDANYD GKDYNPLLAR QGQDVAPPPN PGDQIFNKSK KLIGTAVPQR TSPTGPKNMQ TSGRLSNVAP PCILRKNPPS ARNGGHETDA QILELNQQLV DLKLTVDGLE KERDFYFSKL RDIELICQEH ESENSPVISG IIGILYATEE GFAPPEDDEI EEHQQEDQDE Y
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 :
RELM g MouseDescription:
RELM-Gamma Mouse Recombinant
Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.
Product # :
CYT-1035Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
RELM g Mouse Recombinant produced in E.Coli is a non glycosylated, homodimeric polypeptide chain containing 2 x 89 amino acids and having a total molecular mass of 18.9kDa. The RELM is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a sterile filtered solution containing 0.1 % trifluoroacetic acid (TFA).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
RELM-gamma is a novel member of the resistin-like molecule/found in inflammatory zone (RELM/FIZZ) family in mice and rats. Microarray and real-time RT-PCR experiments revealed a repression of RELMgamma mRNA in nasal respiratory epithelium of cigarette smoke-exposed versus untreated rats. The analysis of the physiological tissue-specific expression revealed highest expression in hematopoietic tissues, suggesting a cytokine-like role for RELM-gamma. RELM-gamma-mRNA is detectable in bone marrow, spleen, and lung as well as in peripheral blood granulocytes. Promyelocytic HL60 cells transfected with a RELM-gamma expression plasmid have an increased proliferation rate compared to mock-transfected cells and display an altered response to retinoic acid-induced granulocytic differentiation. Taken together, these data provide the first experimental evidence that RELM-gamma is a secreted molecule with a restricted expression pattern that may play a role in promyelocytic differentiation.
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Synonyms
Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized RELM g although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution RELM g Mouse 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 RELM g in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MEGTLESIVE KKVKELLANR DDCPSTVTKT FSCTSITASG RLASCPSGMT VTGCACGYGC GSWDIRDGNT CHCQCSTMDW ATARCCQLA.
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 :
RLBP1 HumanDescription:
Retinaldehyde Binding Protein 1 Human Recombinant
Retinaldehyde Binding Protein 1, Cellular Retinaldehyde-Binding Protein, CRALBP.
Product # :
PRO-1845Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RLBP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 340 amino acids (1-317) and having a molecular mass of 38.9 kDa. RLBP1 is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The RLBP1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
RLBP1 is a 36-kD water-soluble protein that transports 11-cis-retinal or 11-cis-retinaldehyde as physiologic ligands. RLBP1 is a functional element of the visual cycle. RLBP1 gene mutations cause retinitis punctata albescens, severe rod-cone dystrophy and Bothnia dystrophy (nonsyndromic autosomal recessive retinitis pigmentosa).
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Synonyms
Retinaldehyde Binding Protein 1, Cellular Retinaldehyde-Binding Protein, CRALBP.
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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
MGSSHHHHHH SSGLVPRGSH MGSMSEGVGT FRMVPEEEQE LRAQLEQLTT KDHGPVFGPC SQLPRHTLQK AKDELNEREE TREEAVRELQ EMVQAQAASG EELAVAVAER VQEKDSGFFL RFIRARKFNV GRAYELLRGY VNFRLQYPEL FDSLSPEAVR CTIEAGYPGV LSSRDKYGRV VMLFNIENWQ SQEITFDEIL QAYCFILEKL LENEETQING FCIIENFKGF TMQQAASLRT SDLRKMVDML QDSFPARFKA IHFIHQPWYF TTTYNVVKPF LKSKLLERVF VHGDDLSGFY QEIDENILPS DFGGTLPKYD GKAVAEQLFG PQAQAENTAF
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 :
T.gondii p30Description:
Toxoplasma Gondii p30 (SAG1) Recombinant
Product # :
TOX-264Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
T.gondii p30 is highly conformational antigen containing 12 cysteine residues and is fused to a 6 x His tag at its C-terminus.
Source
Escherichia Coli.
Formulation
PBS, 25mM K2CO3 and 0.025% NaN3.
Purity
Toxoplasma protein is >95% pure as determined by 10% PAGE (coomassie staining).
Citations
More Info
-
Introduction
The life cycle of Toxoplasma gondii has two phases. The coccidia like takes place only in members of the Felidae family which makes these animals the parasite's primary host. The asexual part of the life cycle can take place in any warm-blooded animal, like other mammals(including felines) and birds. T. gondii constructing daughter scaffolds within the mother cell. In the intermediate hosts (including felines), the parasite invades cells, forming intracellular so-called parasitophorous vacuoles containing bradyzoites, the slowly replicating form of the parasit. Vacuoles form tissue cysts mainly within the muscles and brain. Since they are within cells, the host's immune system does not detect these cysts. Resistance to antibiotics varies, but the cysts are very difficult to eradicate entirely. Within these vacuoles T. gondii propagates by a series of binary fissions until the infected cell eventually bursts and tachyzoites are released. Tachyzoites are the motile, asexually reproducing form of the parasite. Unlike the bradyzoites, the free tachyzoites are usually efficiently cleared by the host's immune response, although some manage to infect cells and form bradyzoites, thus maintaining the infection.
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Stability
Toxoplasma protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Applications
Immunoassay.
-
Purification Method
Toxoplasma protein was purified by proprietary chromatographic technique.
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 :
CTF2P MouseDescription:
Neuropoietin Mouse Recombinant
Cardiotrophin-2, CT-2, Neuropoietin, Np, Ctf2, Gm494.
Product # :
CYT-1128Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Neuropoietin Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 182 amino acids and having a molecular mass of approximately 19.7kDa.CTF2P is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 0.5mM DTT and 500mM NaCl.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a cell proliferation assay using human TF-1 cells is < 200 ng/ml, corresponding to a specific activity of > 5000 IU/mg.
Citations
More Info
-
Introduction
CTF2P, aka Neuropoietinis a part of the IL-6 family of cytokines. CTF2P is the outcome of a gene duplication event involving cardiotrophin-1 (CT-1) and it helps to define a subfamily within the IL-6 family that includes CT-1, CLC and CTNF. CTF2P Increases the platelet count associated with splenomegaly and takes part in neuronal precursor development and maturation.
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Synonyms
Cardiotrophin-2, CT-2, Neuropoietin, Np, Ctf2, Gm494.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized CTF2P although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Neuropoietin 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 Neuropoietin in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
APISPSEPIG QAYSLALYMQ KNTSALLQTY LQHQGSPFSD PGFSAPELQL STLPSAAVSF KTWHAMEDAE RLSRAQGAFL ALTQHLQLVG DDQSYLNPGS PILLAQLGAA RLRAQGLLGN MAAIMTALGL PIPPEEDTLG FVPFGASAFE RKCRGYIVTR EYGHWTDRAV RDLALLKAKY SA.
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Background
What is the molecular weight/Mw of CTF2P Protein?
CTF2P Protein has a total Mw of 19.7kDa.
What is the source or expression system of CTF2P Protein?
Escherichia Coli.
What is the Purity of CTF2P Protein?
CTF2P Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of CTF2P Protein?
The ED50 as determined by a cell proliferation assay using human TF-1 cells is < 200 ng/ml, corresponding to a specific activity of > 5000 IU/mg.
What is the amino acid sequence of CTF2P Protein?
APISPSEPIG QAYSLALYMQ KNTSALLQTY LQHQGSPFSD PGFSAPELQL STLPSAAVSF KTWHAMEDAE RLSRAQGAFL ALTQHLQLVG DDQSYLNPGS PILLAQLGAA RLRAQGLLGN MAAIMTALGL PIPPEEDTLG FVPFGASAFE RKCRGYIVTR EYGHWTDRAV RDLALLKAKY SA.
What applications can CTF2P Protein be used in?
CTF2P Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CTF2P Protein?
The endotoxin level is minimal, CTF2P 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 :
Aprotinin ProteinDescription:
Aprotinin
Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.
Product # :
PRO-285Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Aprotinin is a natural proteinase inhibitor polypeptide consisting of fifty-eight amino acids {C284H432N84O79S7} arranged in a single polypeptide chain, cross-linked by three disulfide bridges and having a molecular mass of 6512.
Source
Bovine Lung.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Citations
More Info
-
Introduction
Aprotinin inhibits the activity of several proteolytic enzymes such as chymotrypsin, kallikrein, plasmin and trypsin. Aprotinin is present in blood and in most tissues, with a high concentration in lung. Aprotinin inhibits pro-inflammatory cytokine release and maintains glycoprotein homeostasis. In platelets, aprotinin reduces glycoprotein loss (e.g., GpIb, GpIIb/IIIa), while in granulocytes it prevents the expression of pro-inflammatory adhesive glycoproteins (e.g., CD11b).
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Synonyms
Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Aprotinin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Aprotinin 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.
-
Solubility
It is recommended to reconstitute the lyophilized Aprotinin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Specific Activity
5,940 KIU (Kallikrein Inactivator Units) per mg, 3.3 pH.Eur.U/mg.
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 :
SIT1 HumanDescription:
Signaling Threshold Regulating Transmembrane Adaptor 1 Human Recombinant
Signaling threshold-regulating transmembrane adapter 1, SHP2-interacting transmembrane adapter protein, Suppression-inducing transmembrane adapter 1, gp30/40, SIT1, SIT, RP11-331F9.5, MGC125908, MGC125909, MGC125910.
Product # :
PRO-928Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SIT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (62-196 a.a.) and having a molecular mass of 16.9kDa (Molecular weight on SDS-PAGE will appear higher).SIT1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SIT1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Signaling threshold-regulating transmembrane adapter 1 (SIT1) negatively regulates T-cell antigen receptor (TCR)-mediated signaling in T-cells. SIT1 is involved in positive selection of T-cells. SIT1 is specifically expressed in T- and B-cells. SIT1 is also present in plasma cells but not in germinal center B-cells (at protein level). SIT1 is expressed in T- and B-cell lymphoma.
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Synonyms
Signaling threshold-regulating transmembrane adapter 1, SHP2-interacting transmembrane adapter protein, Suppression-inducing transmembrane adapter 1, gp30/40, SIT1, SIT, RP11-331F9.5, MGC125908, MGC125909, MGC125910.
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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 MHLSQWTRGR SRSHPGQGRS GESVEEVPLY GNLHYLQTGR LSQDPEPDQQ DPTLGGPARA AEEVMCYTSL QLRPPQGRIP GPGTPVKYSE VVLDSEPKSQ ASGPEPELYA SVCAQTRRAR ASFPDQAYAN SQPAAS.
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 :
TBC1D22B HumanDescription:
TBC1 Domain Family, Member 22B Human Recombinant
TBC1 Domain Family, Member 22B, C6orf197, Chromosome 6 Open Reading Frame 197, TBC1 Domain Family Member 22B, TBC1 domain family member 22B.
Product # :
PRO-2214Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TBC1D22B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 528 amino acids (1-505 a.a) and having a molecular mass of 61.5kDa. TBC1D22B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TBC1D22B protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4) 30% glycerol and 1mM DTT.
Purity
Greater than 80% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
TBC1 domain family member 22B, also known as TBC1D22B acts as a GTPase-activating protein for Rab family protein. The Tre-2/Bub2/Cdc16 (TBC) domain is a conserved protein motif which consists of roughly 200 amino acids and functions as a specific Rab-GAP domain. The TBC domain has more than 40 distinct TBC domain-containing proteins which have been identified in humans.
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Synonyms
TBC1 Domain Family, Member 22B, C6orf197, Chromosome 6 Open Reading Frame 197, TBC1 Domain Family Member 22B, TBC1 domain family member 22B.
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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 MGSMAAENSK QFWKRSAKLP GSIQPVYGAQ HPPLDPRLTK NFIKERSKVN TVPLKNKKAS SFHEFARNTS DAWDIGDDEE EDFSSPSFQT LNSKVALATA AQVLENHSKL RVKPERSQST TSDVPANYKV IKSSSDAQLS RNSSDTCLRN PLHKQQSLPL RPIIPLVARI SDQNASGAPP MTVREKTRLE KFRQLLSSQN TDLDELRKCS WPGVPREVRP ITWRLLSGYL PANTERRKLT LQRKREEYFG FIEQYYDSRN EEHHQDTYRQ IHIDIPRTNP LIPLFQQPLV QEIFERILFI WAIRHPASGY VQGINDLVTP FFVVFLSEYV EEDVENFDVT NLSQDMLRSI EADSFWCMSK LLDGIQDNYT FAQPGIQKKV KALEELVSRI DEQVHNHFRR YEVEYLQFAF RWMNNLLMRE LPLRCTIRLW DTYQSEPEGF SHFHLYVCAA FLIKWRKEIL DEEDFQGLLM LLQNLPTIHW GNEEIGLLLA EAYRLKYMFA DAPNHYRR.
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 :
TNF a CanineDescription:
Tumor Necrosis Factor-Alpha Canine Recombinant
Tumor necrosis factor, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, TNFA, TNFSF2.
Product # :
CYT-140Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TNF-a Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 157 amino acids and having a molecular mass of 17.3 kDa. The TNF-a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 1×PBS, pH7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Specific Activity is >3.3×105 IU/mg as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D.Citations
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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer. -
Synonyms
Tumor necrosis factor, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, TNFA, TNFSF2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a 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 Tumor Necrosis Factor-alpha 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
VKSSSRTPSD KPVAHVVANP EAEGQLQWLS RRANALLANG VELTDNQLIV PSDGLYLIYS QVLFKGQGCP STHVLLTHTI SRFAVSYQTK VNLLSAIKSP CQRETPEGTE AKPWYEPIYL GGVFQLEKGD RLSAEINLPN YLDFAESGQV YFGIIAL.
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 :
TNFSF12 HumanDescription:
TNF Ligand Superfamily Member 12 Human Recombinant
TWEAK, TNF-related weak inducer of apoptosis, TNFSF12, DR3LG, Apo3-Ligand, APO3L, TNFRSF12A, Tumor necrosis factor ligand superfamily member 12, MGC20669, MGC129581.
Product # :
CYT-699Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TNFSF12 Human Recombinant (94-249 a.a.) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 156 amino acids and having a total molecular mass of 18kDa. The TNFSF12 is fused with an 8 amino acids his tag at N-terminal (M-HHHHHH-R, total 164 a.a.) and purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
Lyophilized from a 0.2μm filtered solution in PBS.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured in a proliferation assay using HUVECs, is less than 8ng/ml.
Citations
More Info
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Introduction
TNFSF12 is a cytokine that is part of the TNF ligand family. TNFSF12 is a ligand for the FN14/TWEAKR receptor. TNFSF12 has overlapping signaling functions with TNF, but displays a much wider tissue distribution. TNFSF12 induces apoptosis through multiple pathways of cell death in a cell type-specific manner. TNFSF12 promotes proliferation and migration of endothelial cells, and therefore acts as a regulator of angiogenesis. TNFSF12 is expressed in adult heart, pancreas, skeletal muscle, small intestine, spleen and peripheral blood lymphocytes. TWEAK h induces NFkB and chemokine secretion. TNFSF12 exerts an apoptotic activity in HT-29 human adenocarcinoma cells whilst cultured in the presence of IFN-?. TNFSF12 promotes proliferation and migration of endothelial cells.
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Synonyms
TWEAK, TNF-related weak inducer of apoptosis, TNFSF12, DR3LG, Apo3-Ligand, APO3L, TNFRSF12A, Tumor necrosis factor ligand superfamily member 12, MGC20669, MGC129581.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TNFSF12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TWEAK 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 TNFSF12 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
MHHHHHHRSA PKGRKTRARR AIAAHYEVHP RPGQDGAQAG VDGTVSGWEE ARINSSSPLR YNRQIGEFIV TRAGLYYLYC QVHFDEGKAV YLKLDLLVDG VLALRCLEEF SATAASSLGP QLRLCQVSGL LALRPGSSLR IRTLPWAHLK AAPFLTYFGL FQVH.
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 :
SHH (C24II) HumanDescription:
Sonic HedgeHog (C24II) Human Recombinant
Sonic Hedgehog, MCOPCB5, SMMCI, HLP3, HPE3, Sonic Hedgehog (Drosophila) Homolog, Sonic Hedgehog Homolog (Drosophila), Sonic Hedgehog Homolog, Sonic Hedgehog Protein, TPTPS, HHG-1, HHG1, TPT, SHH (C24II).
Product # :
CYT-888Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SHH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 176 amino acids (24-197 a.a.) and having a molecular mass of 19.8kDa (The Cys at position 24 has been replaced with 2 Ile).The SHH is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SHH protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4).
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Sonic Hedgehog is part of a small group of secreted proteins which are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog is a protein that is vital in guding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which functions in association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is essential for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.
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Synonyms
Sonic Hedgehog, MCOPCB5, SMMCI, HLP3, HPE3, Sonic Hedgehog (Drosophila) Homolog, Sonic Hedgehog Homolog (Drosophila), Sonic Hedgehog Homolog, Sonic Hedgehog Protein, TPTPS, HHG-1, HHG1, TPT, SHH (C24II).
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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
MIIGPGRGFG KRRHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKISRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRSKYGML ARLAVEAGFD WVYYESKAHI HCSVKAENSV AAKSGG
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 :
HSPBP1 HumanDescription:
Heat Shock Protein-Binding Protein 1 Human Recombinant
Hsp70-binding protein 1, Heat shock protein-binding protein 1, Hsp70-interacting protein 1, Hsp70-binding protein 2, Hsp70-interacting protein 2, HspBP1, HspBP2, HSPBP1, HSPBP, FES1.
Product # :
HSP-030Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
HSPBP1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 382 amino acids (1-362 a.a.) and having a molecular mass of 41.6kDa. HSPBP1 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HSPBP1 solution containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 30% glycerol, 2mM EDTA and 0.1M NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Hsp70-binding protein 1 (HSPBP1) is a member of a family of eukaryotic proteins identified as nucleotide exchange factors for HSP 70 that exhibit varying degrees of compartment and species specificity. HSPBP1 is localized mainly in cytoplasm and nucleus but is also found extracellularly. HSPBP1 is mostly expressed in heart and skeletal muscle .HSPBP1 binds to HSP 70, inhibits its activity and promotes dissociation of nucleotides from the HSP 70 ATPase domain. In addition, HSPBP1 inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and obstructing the ATP binding. HSPBP1 may also have a role in tumor (dys)regulation of chaperone proteins. Furthermore, HSPBP1 hinders ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR.
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Synonyms
Hsp70-binding protein 1, Heat shock protein-binding protein 1, Hsp70-interacting protein 1, Hsp70-binding protein 2, Hsp70-interacting protein 2, HspBP1, HspBP2, HSPBP1, HSPBP, FES1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
HSPBP1 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSDEGSRGSR LPLALPPASQ GCSSGGGGGG GGGSSAGGSG NSRPPRNLQG LLQMAITAGS EEPDPPPEPM SEERRQWLQE AMSAAFRGQR EEVEQMKSCL RVLSQPMPPT AGEAEQAADQ QEREGALELL ADLCENMDNA ADFCQLSGMH LLVGRYLEAG AAGLRWRAAQ LIGTCSQNVA AIQEQVLGLG ALRKLLRLLD RDACDTVRVK ALFAISCLVR EQEAGLLQFL RLDGFSVLMR AMQQQVQKLK VKSAFLLQNL LVGHPEHKGT LCSMGMVQQL VALVRTEHSP FHEHVLGALC SLVTDFPQGV RECREPELGL EELLRHRCQL LQQHEEYQEE LEFCEKLLQT CFSSPADDSM DR.
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.