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Name :
Streptavidin, HisDescription:
Streptavidin Recombinant, His Tag
Product # :
PRO-621Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Streptomyces Avidinii Streptavidin produced in E.Coli is a single, non-glycosylated polypeptide chain (25-183) containing a total of 167 amino acids and having a molecular mass of 17kDa. The Streptavidin protein is fused to an 8 aa N-terminal His-Tag and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Streptavidin protein solution (1mg/ml) contains 20mM Tris-HCl pH7.5.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Citations
More Info
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Introduction
Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is widely used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.
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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
MVHHHHHHDP SKDSKAQVSA AEAGITGTWY NQLGSTFIVT AGADGALTGT YESAVGNAES RYVLTGRYDS APATDGSGTA LGWTVAWKNN YRNAHSATTW SGQYVGGAEA RINTQWLLTS GTTEANAWKS TLVGHDTFTK VKPSAASIDA AKKAGVNNGN PLDAVQQ.
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 :
PALM HumanDescription:
Paralemmin Human Recombinant
Paralemmin-1, Paralemmin, PALM, KIAA0270, Paralemmin-1 isoform 1.
Product # :
PRO-2053Price :
Quantity :
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Shipped with Ice Packs
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Description
PALM Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (1-387) and having a molecular mass of 44.5kDa.PALM is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The PALM solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Paralemmin (PALM) belongs to the paralemmin protein family which takes part in plasma membrane dynamics and cell process formation. The product of PALM is related with the cytoplasmic face of plasma membranes and is implicated in plasma membrane dynamics in neurons and other cell types.
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Synonyms
Paralemmin-1, Paralemmin, PALM, KIAA0270, Paralemmin-1 isoform 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 MGSMEVLAAE TTSQQERLQA IAEKRKRQAE IENKRRQLED ERRQLQHLKS KALRERWLLE GTPSSASEGD EDLRRQMQDD EQKTRLLEDS VSRLEKEIEV LERGDSAPAT AKENAAAPSP VRAPAPSPAK EERKTEVVMN SQQTPVGTPK DKRVSNTPLR TVDGSPMMKA AMYSVEITVE KDKVTGETRV LSSTTLLPRQ PLPLGIKVYE DETKVVHAVD GTAENGIHPL SSSEVDELIH KADEVTLSEA GSTAGAAETR GAVEGAARTT PSRREITGVQ AQPGEATSGP PGIQPGQEPP VTMIFMGYQN VEDEAETKKV LGLQDTITAE LVVIEDAAEP KEPAPPNGSA AEPPTEAASR EENQAGPEAT TSDPQDLDMK KHRCKCCSIM.
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 :
TGIF2LX HumanDescription:
TGFB-Induced Factor Homeobox 2-Like, X-Linked Human Recombinant
Homeobox protein TGIF2LX, TGF-beta-induced transcription factor 2-like protein, TGFB-induced factor 2-like protein, X-linked, TGIF-like on the X, TGIF2LX, TGIFLX, TGFB-Induced Factor Homeobox 2-Like, X-Linked.
Product # :
PRO-1902Price :
Quantity :
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Shipped with Ice Packs
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Description
TGIF2LX Human Recombinant produced in E. coli is. a single polypeptide chain containing 264 amino acids (1-241) and having a molecular mass of 29.1kDa.TGIF2LX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TGIF2LX solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TGFB-Induced Factor Homeobox 2-Like, X-Linked (TGIF2LX) belongs to the TALE/TGIF homeobox family of transcription factors and takes part in spermatogenesis. A homolog of TGIF2LX is located in the male specific region of chromosome Y, in a block of sequence which is the outcome of a large X-to-Y transposition.
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Synonyms
Homeobox protein TGIF2LX, TGF-beta-induced transcription factor 2-like protein,
TGFB-induced factor 2-like protein, X-linked, TGIF-like on the X, TGIF2LX, TGIFLX, TGFB-Induced Factor Homeobox 2-Like, X-Linked. -
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 MGSMEAAADG PAETQSPVEK DSPAKTQSPA QDTSIMSRNN ADTGRVLALP EHKKKRKGNL PAESVKILRD WMYKHRFKAY PSEEEKQMLS EKTNLSLLQI SNWFINARRR ILPDMLQQRR NDPIIGHKTG KDAHATHLQS TEASVPAKSG PSGPDNVQSL PLWPLPKGQM SREKQPDPES APSQKLTGIA QPKKKVKVSV TSPSSPELVS PEEHADFSSF LLLVDAAVQR AAELELEKKQ EPNP.
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 :
TRAF1 HumanDescription:
TNF receptor-Associated Factor 1 Human Recombinant
TRAF-1, EBI6, Epstein-Barr virus-induced protein 6, TNF Receptor-Associated Factor 1, MGC:10353.
Product # :
PRO-834Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TRAF1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 172 amino acids (266-416 a.a.) and having a molecular mass of 19.5 kDa. TRAF1 protein is fused to a 21 amino acid His tag at N-terminus and is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
TRAF1 Human solution containing 20mM Tris-HCl pH-8, 0.1M NaCl, 1mM DTT & 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TRAF1 is an adapter protein and signal transducer that connects members of the TNFR family to different signaling pathways by association with the receptor cytoplasmic domain and kinases. TRAF1 mediates activation of NF-kappa-B and JNK and participates in apoptosis. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2.
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Synonyms
TRAF-1, EBI6, Epstein-Barr virus-induced protein 6, TNF Receptor-Associated Factor 1, MGC:10353.
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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 MDGTFLWKIT NVTRRCHESA CGRTVSLFSP AFYTAKYGYK LCLRLYLNGD GTGKRTHLSL FIVIMRGEYD ALLPWPFRNK VTFMLLDQNN REHAIDAFRP DLSSASFQRP QSETNVASGC PLFFPLSKLQ SPKHAYVKDD TMFLKCIVET ST.
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 :
LITAF HumanDescription:
Lipopolysaccharide-Induced TNF Factor Human Recombinant
Lipopolysaccharide-induced TNF-alpha factor, PIG7, SIMPLE, Lipopolysaccharide-induced tumor necrosis factor-alpha factor, LPS-induced TNF-alpha factor, p53-induced gene 7 protein, Small integral membrane protein of lysosome/late endosome, LITAF.
Product # :
PRO-1350Price :
Quantity :
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Shipped with Ice Packs
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Description
LITAF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (1-161) and having a molecular mass of 19.2 kDa. LITAF is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LITAF solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Lipopolysaccharide-induced TNF-alpha factor (LITAF) is a small integral membrane protein of lysosome/late endosome. The expression of inflammatory cytokines such as TNF-alpha in Lipopolysaccharide-induced processes is mediated by LITAF. LITAF connects to STAT6B, which belongs to the STAT6 family forming a complex on the TNF-alpha promoter that modifies TNF activity. High levels of expression of LITAF mRNA are observed mostly in the placenta, peripheral blood leukocytes, lymph nodes and spleen.
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Synonyms
Lipopolysaccharide-induced TNF-alpha factor, PIG7, SIMPLE, Lipopolysaccharide-induced tumor necrosis factor-alpha factor, LPS-induced TNF-alpha factor, p53-induced gene 7 protein, Small integral membrane protein of lysosome/late endosome, LITAF.
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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 MSVPGPYQAA TGPSSAPSAP PSYEETVAVN SYYPTPPAPM PGPTTGLVTG PDGKGMNPPS YYTQPAPIPN NNPITVQTVY VQHPITFLDR PIQMCCPSCN KMIVSQLSYN AGALTWLSCG SLCLLGCIAG CCFIPFCVDA LQDVDHYCPN CRALLGTYKR L.
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 :
CXCL5 Mouse LIXDescription:
LIX Mouse Recombinant (CXCL5)
C-X-C motif chemokine 5, Small-inducible cytokine B5, Cytokine LIX, Cxcl5, Scyb5, LIX, GCP-2, Scyb6, ENA-78, AMCF-II.
Product # :
CHM-031Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
LIX Mouse (CXCL5) Recombinant (49-118) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 74 amino acids and having a molecular mass of 8kDa.The LIX Mouse is expressed with 4 additional amino acids [VIAA] at n-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LIX Mouse is lyophilized from a 0.2µm filtered solution in PBS.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured by its ability to chemoattract human CXCR2-transfected mouse BaF3 cells, is less than 0.1µg/ml.Citations
More Info
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Introduction
Chemokine (C-X-C motif) ligand 5 (CXCL5) is a small cytokine belonging to the CXC chemokine family that is also known as epithelial-derived neutrophil-activating peptide 78 (ENA-78). It is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. Expression of CXCL5 has also been observed in eosinophils, and can be inhibited with the type II IFN. This chemokine stimulates the chemotaxis of neutrophils possesses angiogenic properties. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2. The gene for CXCL5 is encoded on four exons and is located on human chromosome 4 amongst several other CXC chemokine genes. CXCL5 has been implicated in connective tissue remodelling.
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Synonyms
C-X-C motif chemokine 5, Small-inducible cytokine B5, Cytokine LIX, Cxcl5, Scyb5, LIX, GCP-2, Scyb6, ENA-78, AMCF-II.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized LIX Mouse although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL5 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 LIX Mouse 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
VIAATELRCV CLTVTPKINP KLIANLEVIP AGPQCPTVEV IAKLKNQKEV CLDPEAPVIK KIIQKILGSD KKKA.
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Background
What is the molecular weight/Mw of CXCL5 MOUSE LIX Protein?
CXCL5 MOUSE LIX Protein has a total Mw of 8kDa.
What is the source or expression system of CXCL5 MOUSE LIX Protein?
Escherichia Coli.
What is the Purity of CXCL5 MOUSE LIX Protein?
CXCL5 MOUSE LIX Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL5 MOUSE LIX Protein?
The ED50, as measured by its ability to chemoattract human CXCR2-transfected mouse BaF3 cells, is less than 0.1µg/ml.
What is the amino acid sequence of CXCL5 MOUSE LIX Protein?
VIAATELRCV CLTVTPKINP KLIANLEVIP AGPQCPTVEV IAKLKNQKEV CLDPEAPVIK KIIQKILGSD KKKA.
What applications can CXCL5 MOUSE LIX Protein be used in?
CXCL5 MOUSE LIX Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL5 MOUSE LIX Protein?
The endotoxin level is minimal, CXCL5 MOUSE LIX Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL5 MOUSE LIX 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 CXCL5 MOUSE LIX?
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 :
RBM18 HumanDescription:
RNA Binding Motif Protein 18 Human Recombinant
RNA Binding Motif Protein 18, RNA-Binding Motif Protein 18, RBM18.
Product # :
PRO-2109Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RBM18 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213 amino acids (1-190 a.a) and having a molecular mass of 24kDa.RBM18 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RBM18 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
RNA Binding Motif Protein 18 (RBM18) is comprised of one RNA recognition motif (RRM) domain.
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Synonyms
RNA Binding Motif Protein 18, RNA-Binding Motif Protein 18, RBM18.
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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 MGSMEAETKT LPLENASILS EGSLQEGHRL WIGNLDPKIT EYHLLKLLQK FGKVKQFDFL FHKSGALEGQ PRGYCFVNFE TKQEAEQAIQ CLNGKLALSK KLVVRWAHAQ VKRYDHNKND KILPISLEPS SSTEPTQSNL SVTAKIKAIE AKLKMMAENP DAEYPAAPVY SYFKPPDKKR TTPYSRTAWK SRR.
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 :
RLN2 HumanDescription:
Relaxin-2 Human Recombinant
Prorelaxin H2, RLN2, H2, RLXH2, H2-RLX, bA12D24.1.1, bA12D24.1.2.
Product # :
PRO-1327Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
RLN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 184 amino acids (25-185 a.a) and having a molecular mass of 20.7kDa.RLN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RLN2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Prorelaxin H2 (RLN2) is a member of a family which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. It may also have other roles in boosting sperm motility, regulating blood pressure, controlling heart rate and releasing vasopressin. RLN2 is a peptide hormone linked to several therapeutically relevant physiological effects, including regulation of collagen metabolism and multiple vascular control pathways. The active form of the RLN2 protein consists of an A chain and a B chain linked by disulfide bonds.
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Synonyms
Prorelaxin H2, RLN2, H2, RLXH2, H2-RLX, bA12D24.1.1, bA12D24.1.2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDSWMEEV IKLCGRELVR AQIAICGMST WSKRSLSQED APQTPRPVAE IVPSFINKDT ETINMMSEFV ANLPQELKLT LSEMQPALPQ LQQHVPVLKD SSLLFEEFKK LIRNRQSEAA DSSPSELKYL GLDTHSRKKR QLYSALANKC CHVGCTKRSL ARFC.
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 :
HEXIM1 HumanDescription:
Hexamethylene Bis-Acetamide Inducible 1 Human Recombinant
CLP1, EDG1, HIS1, MAQ1, Protein HEXIM1, Hexamethylene bis-acetamide-inducible protein 1, Estrogen down-regulated gene 1 protein, Cardiac lineage protein 1, Menage a quatre protein 1, FLJ13562.
Product # :
PRO-789Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HEXIM1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 396 amino acids (1-359a.a.) and having a molecular mass of 44.8 kDa. HEXIM1 is fused to a 37 amino acid His-Tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HEXIM1 solution (0.5mg/ml) containing 20mM Tris-HCl pH-8, 0.1M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
HEXIM1 expression is induced by hexamethylene-bis-acetamide in vascular smooth muscle cells. HEXIM1 is a transcriptional regulator which acts as a universal RNA polymerase II transcription inhibitor. In cooperation with 7SK snRNA sequesters P-TEFb in a large inactive 7SK snRNP complex inhibits RNA polymerase II phosphorylation following transcriptional elongation. HEXIM1 regulates NF-kappa-B, ESR1, NR3C1 and CIITA-dependent transcriptional activity.
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Synonyms
CLP1, EDG1, HIS1, MAQ1, Protein HEXIM1, Hexamethylene bis-acetamide-inducible protein 1, Estrogen down-regulated gene 1 protein, Cardiac lineage protein 1, Menage a quatre protein 1, FLJ13562.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMAE PFLSEYQHQP QTSNCTGAAA VQEELNPERP PGAEERVPEE DSRWQSRAFP QLGGRPGPEG EGSLESQPPP LQTQACPESS CLREGEKGQN GDDSSAGGDF PPPAEVEPTP EAELLAQPCH DSEASKLGAP AAGGEEEWGQ QQRQLGKKKH RRRPSKKKRH WKPYYKLTWE EKKKFDEKQS LRASRIRAEM FAKGQPVAPY NTTQFLMDDH DQEEPDLKTG LYSKRAAAKS DDTSDDDFME EGGEEDGGSD GMGGDGSEFL QRDFSETYER YHTESLQNMS KQELIKEYLE LEKCLSRMED ENNRLRLESK RLGGDDARVR ELELELDRLR AENLQLLTEN ELHRQQERAP LSKFGD.
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 :
CCL1 Human, HisDescription:
I-309 (CCL1) Human Recombinant, His Tag
Small inducible cytokine A1, CCL1, T lymphocyte-secreted protein I-309, chemokine (C-C motif) ligand 1, P500, SISe, TCA3, I-309, SCYA1.
Product # :
CHM-254Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
I-309 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 94 amino acids (24-96 a.a.) and having a molecular mass of 10.8kDa. The I-309 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The I-309 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 2mM DTT, 10% glycerol and 50mM NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
SDS-PAGE
Citations
More Info
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Introduction
Chemokine (C-C motif) ligand 1 (CCL1) is a small glycoprotein secreted by activated T cells that belongs to a family inflammatory cytokines known as chemokines. CCL1 attracts monocytes, NK cells, and immature B cells and dendritic cells by interacting with a cell surface chemokine receptor called CCR8. This chemokine resides in a large cluster of CC chemokines on human chromosome 17.
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Synonyms
Small inducible cytokine A1, CCL1, T lymphocyte-secreted protein I-309, chemokine (C-C motif) ligand 1, P500, SISe, TCA3, I-309, SCYA1.
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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 MKSMQVPFSR CCFSFAEQEI PLRAILCYRN TSSICSNEGL IFKLKRGKEA CALDTVGWVQ RHRKMLRHCP SKRK.
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Background
What is the molecular weight/Mw of CCL1 HUMAN, HIS Protein?
CCL1 HUMAN, HIS Protein has a total Mw of 10.8kDa.
What is the source or expression system of CCL1 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CCL1 HUMAN, HIS Protein?
CCL1 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL1 HUMAN, HIS Protein?
The biological functionality of CCL1 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CCL1 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MKSMQVPFSR CCFSFAEQEI PLRAILCYRN TSSICSNEGL IFKLKRGKEA CALDTVGWVQ RHRKMLRHCP SKRK.
What applications can CCL1 HUMAN, HIS Protein be used in?
CCL1 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL1 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL1 HUMAN, HIS Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL1 HUMAN, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CCL1 HUMAN, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
NTS Human, sf9Description:
Neurotensin Human Recombinant, sf9
Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.
Product # :
PRO-2374Price :
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Description
NTS Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 134 amino acids (24-148) and having a molecular mass of 15.4kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).NTS is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
NTS protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by analysis by SDS-PAGE.
Citations
More Info
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Introduction
Neurotensin (NTS) is a common precursor for 2 peptides, neuromedin N and neurotensin. Neurotensin is a secreted tridecapeptide, which is generally distributed throughout the central nervous system, and may serve as a neurotransmitter or a neuromodulator. NTS is involved in dopamine-associated pathophysiological events, in the maintenance of gut structure and function, and in the regulation of fat metabolism. Tissue-specific processing may initiate the formation in some tissues of larger forms of neuromedin N and neurotensin. The large forms may embody more stable peptides which are also biologically active.
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Synonyms
Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.
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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
ADPSDSEEEM KALEADFLTN MHTSKISKAH VPSWKMTLLN VCSLVNNLNS PAEETGEVHE EELVARRKLP TALDGFSLEA MLTIYQLHKI CHSRAFQHWE LIQEDILDTG NDKNGKEEVI KRKIPYILHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL 15 MouseDescription:
Interleukin-15 Mouse Recombinant
IL-15, MGC9721, Interleukin-15, Il15, AI503618.
Product # :
CYT-647Price :
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Description
Interleukin-15 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids (49-162 a.a.) and having a molecular mass of 17.6 kDa. The IL-15 is fused to a 37 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The mouse IL-15 protein solution contains PBS, pH-7.4 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using CTLL2 mouse cytotoxic T cells. The ED50 for this effect is < 1 ng/ml, corresponding to a specific activity of 1,000,000IU/mg.Citations
More Info
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Introduction
The protein encoded by this gene is a cytokine that regulates T and natural killer cell activation and proliferation. This cytokine and interleukine 2 share many biological activities. They are found to bind common hematopoietin receptor subunits, and may compete for the same receptor, and thus negatively regulate each other's activity. The number of CD8+ memory cells is shown to be controlled by a balance between this cytokine and IL2. This cytokine induces the activation of JAK kinases, as well as the phosphorylation and activation of transcription activators STAT3, STAT5, and STAT6. Studies of the mouse counterpart suggested that this cytokine may increase the expression of apoptosis inhibitor BCL2L1/BCL-x(L), possibly through the transcription activation activity of STAT6, and thus prevent apoptosis. Two alternatively spliced transcript variants of this gene encoding the same protein have been reported.
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Synonyms
IL-15, MGC9721, Interleukin-15, Il15, AI503618.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMNW IDVRYDLEKI ESLIQSIHID TTLYTDSDFH PSCKVTAMNC FLLELQVILH
EYSNMTLNET VRNVLYLANS TLSSNKNVAE SGCKECEELE EKTFTEFLQS FIRIVQMFIN TS.
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 :
OSM HumanDescription:
Oncostatin-M Human Recombinant
OSM, MGC20461.
Product # :
CYT-231Price :
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Shipped at Room temp
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Description
Oncostatin-M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids and having a molecular mass of 26kDa. The OSM is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing PBS pH-7.4.
Purity
Greater than 95.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of Human TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000IU/mg.Citations
More Info
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Introduction
Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.
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Synonyms
OSM, MGC20461.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Oncostatin M although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin 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 Oncostatin M 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
AAIGSCSKEY RVLLGQLQKQ TDLMQDTSRL LDPYIRIQGL DVPKLREHCR
ERPGAFPSEE TLRGLGRRGF LQTLNATLGC VLHRLADLEQ RLPKAQDLER
SGLNIEDLEK LQMARPNILG LRNNIYCMAQ LLDNSDTAEP TKAGRGASQP
PTPTPASDAF QRKLEGCRFL HGYHRFMHSV GRVFSKWGES PNRSRRHSPH
QALRKGVRRT RPSRKGKRLM TRGQLPR. -
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.45 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using standard solution of Oncostatin as Reference.
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 :
STMN2 HumanDescription:
Stathmin Like-2 Human Recombinant
SCG10, STMB2, SCGN10, AI159727, STMN-2, Stathmin-2, Superior cervical ganglion-10 protein, Protein SCG10, STMN2, SGC10, stathmin-like 2.
Product # :
PRO-752Price :
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Description
Recombinant Human Stathmin Like-2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 142 amino acids (39-179 a.a) and having a molecular mass of 16.4 kDa. STMN2 is purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The STMN2 protein solution contains 50mM MES, pH-6.0, 0.1mM PMSF, 1 mM EDTA and 10% Glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
STMN2 is a neuronal growth-associated protein which shares a majority of its amino acid sequence with the phosphoprotein stathmin. STMN2 is involved in neuronal differentiation and in modulating membrane interaction with the cytoskeleton through neurite outgrowth. STMN2 is necessary for maintaining the anchorage-independent growth state of beta-catenin/TCF-activated hepatoma cells. SCG10 is a novel indicator of osteogenesis and osteoblast that takes part in the regulation of the adipocyte/osteoblast balance. STMN2 plays a role as an effector downstream of Rnd1 to regulate axon extensions by modulating microtubule organization.
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Synonyms
SCG10, STMB2, SCGN10, AI159727, STMN-2, Stathmin-2, Superior cervical ganglion-10 protein, Protein SCG10, STMN2, SGC10, stathmin-like 2.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MDMEVKQINK RASGQAFELI LKPPSPISEA PRTLASPKKK DLSLEEIQKK LEAAEERRKS QEAQVLKQLA EKREHEREVL QKALEENNNF SKMAEEKLIL KMEQIKENRE ANLAAIIERL QEKERHAAEV RRNKELQVEL SG.
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 :
TBPL1 HumanDescription:
TBP-Like 1 Human Recombinant
TATA box-binding protein-like protein 1, TBP-like protein 1, 21 kDa TBP-like protein, Second TBP of unique DNA protein, STUD, TATA box-binding protein-related factor 2, TBP-related factor 2, TBP-like factor, TBP-related protein, TBPL1, TLF, TLP, TLP21, TRF2, TRP, MGC:8389, MGC:9620.
Product # :
PRO-736Price :
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Description
TBPL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 209 amino acids (1-186 a.a) and having a molecular mass of 23.3kDa.TBPL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TBPL1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 2mM DTT and 1mM EDTA.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TBP-Like 1 (TBPL1) is a member of the TBP family. The TATA box-binding protein (TBP) is an indispensable component of the basal transcriptional machinery. TBPL1 is crucial for spermiogenesis and supposed to be significant in expression of developmentally regulated genes.
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Synonyms
TATA box-binding protein-like protein 1, TBP-like protein 1, 21 kDa TBP-like protein, Second TBP of unique DNA protein, STUD, TATA box-binding protein-related factor 2, TBP-related factor 2, TBP-like factor, TBP-related protein, TBPL1, TLF, TLP, TLP21, TRF2, TRP, MGC:8389, MGC:9620.
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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 MGSMDADSDV ALDILITNVV CVFRTRCHLN LRKIALEGAN VIYKRDVGKV LMKLRKPRIT ATIWSSGKII CTGATSEEEA KFGARRLARS LQKLGFQVIF TDFKVVNVLA VCNMPFEIRL PEFTKNNRPH ASYEPELHPA VCYRIKSLRA TLQIFSTGSI TVTGPNVKAV ATAVEQIYPF VFESRKEIL.
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 :
TIAF1 HumanDescription:
TGFB1-Induced Anti-Apoptotic Factor 1 Human Recombinant
TGFB1-Induced Anti-Apoptotic Factor 1, 12 KDa TGF-Beta-1-Induced Antiapoptotic Factor, Molecule Associated With Jak-3 N-Terminal, KIAA0216, MYO18A, MYSPDZ, MAJN, SPR210.
Product # :
PRO-1211Price :
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Description
TIAF1 Human Recombinant produced in E. coli is a single polypeptide chain containing 152 amino acids (1-115) and having a molecular mass of 16.6 kDa.TIAF1 is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TIAF1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TGFB1-induced anti-apoptotic factor 1 (TIAF1) hinders the cytotoxic effects of TNF-alpha and overexpressed TNF receptor adapters TRADD, FADD, and RIPK1. The TIAF1 protein is involved in TGF-beta1 inhibition of IkappaB-alpha expression and suppression of TNF-mediated IkappaB-alpha degradation. TIAF1 is not detected in normal kidney and liver. TIAF1 is up-regulated in chronic and acute allograft rejection: expressed in the inflammatory infiltrate and in tubular epithelial cells.
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Synonyms
TGFB1-Induced Anti-Apoptotic Factor 1, 12 KDa TGF-Beta-1-Induced Antiapoptotic Factor, Molecule Associated With Jak-3 N-Terminal, KIAA0216, MYO18A, MYSPDZ, MAJN, SPR210.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMSS PSSPFREQSF LCAAGDAGEE SRVQVLKNEV RRGSPVLLGW VEQAYADKCV CGPSAPPAPT PPSLSQRVMC NDLFKVNPFQ LQQFRADPST ASLLLCPGGL DHKLNLRGKA WG
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 :
Follistatin Human, HisDescription:
Follistatin Human Recombinant, His Tag
FST, FS, Activin-binding protein.
Product # :
CYT-029Price :
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Shipped at Room temp
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Description
FST His Protein is 36.0 kDa protein containing 325 amino acid residues of the FST His and the 10 aa N-Terminal His-tag.
Source
E. coli.
Formulation
FST His Tag was filtered (0.4µm) and lyophilized from 0.5mg/ml supplied in 20mM TRIS and 20mM NaCl, pH 7.5.
Citations
More Info
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Introduction
Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin binds directly to activin and functions as an activin antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).
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Synonyms
FST, FS, Activin-binding protein.
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Stability
Store lyophilized FST His at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted FST His can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Amino Acid Sequence
MKHHHHHHAS GNCWLRQAKN GRCQVLYKTE LSKEECCSTG RLSTSWTEED VNDNTLFKWM IFNGGAPNCI PCKETCENVD CGPGKKCRMN KKNKPRCVCA PDCSNITWKG PVCGLDGKTY RNECALLKAR CKEQPELEVQ YQGRCKKTCR DVFCPGSSTC VVDQTNNAYC VTCNRICPEP ASSEQYLCGN DGVTYSSACH LRKATCLLGR SIGLAYEGKC IKAKSCEDIQ CTGGKKCLWD FKVGRGRCSL CDELCPDSKS DEPVCASDNA TYASECAMKE AACSSGVLLE VKHSGSCNSI SEDTEEEEED EDQDYSFPIS SILEW.
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Background
What is the molecular weight/Mw of FOLLISTATIN HUMAN, HIS Protein?
FOLLISTATIN HUMAN, HIS Protein has a total Mw of 36kDa.
What is the source or expression system of FOLLISTATIN HUMAN, HIS Protein?
Escherichia Coli.
What is the Biological Activity of FOLLISTATIN HUMAN, HIS Protein?
The biological functionality of FOLLISTATIN HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of FOLLISTATIN HUMAN, HIS Protein?
MKHHHHHHAS GNCWLRQAKN GRCQVLYKTE LSKEECCSTG RLSTSWTEED VNDNTLFKWM IFNGGAPNCI PCKETCENVD CGPGKKCRMN KKNKPRCVCA PDCSNITWKG PVCGLDGKTY RNECALLKAR CKEQPELEVQ YQGRCKKTCR DVFCPGSSTC VVDQTNNAYC VTCNRICPEP ASSEQYLCGN DGVTYSSACH LRKATCLLGR SIGLAYEGKC IKAKSCEDIQ CTGGKKCLWD FKVGRGRCSL CDELCPDSKS DEPVCASDNA TYASECAMKE AACSSGVLLE VKHSGSCNSI SEDTEEEEED EDQDYSFPIS SILEW.
What applications can FOLLISTATIN HUMAN, HIS Protein be used in?
FOLLISTATIN HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FOLLISTATIN HUMAN, HIS Protein?
The endotoxin level is minimal, FOLLISTATIN HUMAN, HIS 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 :
TNNI2 HumanDescription:
Troponin I Type 2 Human Recombinant
Troponin I fast skeletal muscle, Troponin I fast-twitch isoform, TNNI2, DA2B, FSSV, fsTnI, AMCD2B.
Product # :
PRO-341Price :
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Description
Skeletal isoforms of Troponin I were suggested to be used as markers of acute and chronic skeletal muscle injuries. In skeletal muscles Troponin I is presented by two forms, slow (21.6 kDa) and fast (21.2 kDa) skeletal. The protein (Fast Skeletal Troponin I) migrates on SDS-PAGE to approximately 26.5kDa.
Source
Escherichia Coli.
Formulation
The protein solution contains 20mM Tris-HCl, 500mM NaCl and 10mM b-ME, pH 7.5.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TNNI2 is a fast-twitch skeletal muscle protein, belongs to the troponin I gene family, and is part of the troponin complex including troponin T, troponin C and troponin I subunits. The troponin complex, together with tropomyosin, is responsible for the calcium-dependent regulation of striated muscle contraction. TNNI2 is also present in vascular smooth muscle and may play a role in regulation of smooth muscle function. Other than muscle tissues, TNNI2 is found in corneal epithelium, cartilage where it is an inhibitor of angiogenesis to inhibit tumor growth and metastasis, and mammary gland where it functions as a coactivator of estrogen receptor-related receptor alpha. Furthermore, TNNI2 suppresses tumor growth in human ovarian carcinoma. Mutations in the TNNI2 gene cause myopathy and distal arthrogryposis type 2B.
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Synonyms
Troponin I fast skeletal muscle, Troponin I fast-twitch isoform, TNNI2, DA2B, FSSV, fsTnI, AMCD2B.
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Physical Appearance
Sterile Filtered colourless liquid formualtion.
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Stability
TNNI2 Human although stable at 10°C for 7 days, should be stored below -18°C.Please prevent 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 :
TROVE2 His HumanDescription:
TROVE Domain Family Member 2 His Tag Human Recombinant
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
Product # :
PRO-110Price :
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Description
TROVE2 His is a recombinant protein having a molecular mass of 64,000 Dalton (pH 8.3-8.6 (depending on prediction program). TROVE2 is fused to a hexa-histidine purification tag.
Source
Escherichia Coli.
Formulation
TROVE2 is supplied in 20mM HEPES buffer pH-8.0, 150mM NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.
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Synonyms
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
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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. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative samples); line assay and immunodot test with positive/negative samples.
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coating concentration
0.2-0.5 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.
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 :
LGALS9 MouseDescription:
Galectin-9 Mouse Recombinant
Galectin-9, Gal-9, Lgals9, Lgals5, LGALS35, AA407335, AI194909, AI265545.
Product # :
CYT-550Price :
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Description
LGALS9 mouse Recombinant produced E. coli is a single polypeptide chain containing 345 amino acids (1-322) and having a molecular mass of 38kDa.LGALS9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LGALS9 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
SDS-PAGE
Citations
More Info
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Introduction
LGLAS9 binds galactosides and has high affinity for the Forssman pentasaccharide. LGLAS9 participates in thymocyte-epithelial interactions relevant to the biology of the thymus and Inhibits cell proliferation. LGLAS9 is a ligand for HAVCR2/TIM3. LGLAS9 Induces T-helper type 1 lymphocyte (Th1) death. LGLAS9 performs as an eosinophil chemoattractant LGLAS9 is an S-type lectin which is over-expressed in Hodgkin's disease tissue and takes part in the interaction between the H&RS cells with their surrounding cells.
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Synonyms
Galectin-9, Gal-9, Lgals9, Lgals5, LGALS35, AA407335, AI194909, AI265545.
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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 MGSMALFSAQ SPYINPIIPF TGPIQGGLQE GLQVTLQGTT KSFAQRFVVN FQNSFNGNDI AFHFNPRFEE GGYVVCNTKQ NGQWGPEERK MQMPFQKGMP FELCFLVQRS EFKVMVNKKF FVQYQHRVPY HLVDTIAVSG CLKLSFITFQ TQNFRPAHQA PMAQTTIHMV HSTPGQMFST PGIPPVVYPT PAYTIPFYTP IPNGLYPSKS IMISGNVLPD ATRFHINLRC GGDIAFHLNP RFNENAVVRN TQINNSWGQE ERSLLGRMPF SRGQSFSVWI ICEGHCFKVA VNGQHMCEYY HRLKNLQDIN TLEVAGDIQL THVQT.
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Background
What is the molecular weight/Mw of LGALS9 MOUSE Protein?
LGALS9 MOUSE Protein has a total Mw of 38kDa.
What is the source or expression system of LGALS9 MOUSE Protein?
Escherichia Coli.
What is the Purity of LGALS9 MOUSE Protein?
LGALS9 MOUSE Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS9 MOUSE Protein?
The biological functionality of LGALS9 MOUSE Protein will be determined in the future.
What is the amino acid sequence of LGALS9 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMALFSAQ SPYINPIIPF TGPIQGGLQE GLQVTLQGTT KSFAQRFVVN FQNSFNGNDI AFHFNPRFEE GGYVVCNTKQ NGQWGPEERK MQMPFQKGMP FELCFLVQRS EFKVMVNKKF FVQYQHRVPY HLVDTIAVSG CLKLSFITFQ TQNFRPAHQA PMAQTTIHMV HSTPGQMFST PGIPPVVYPT PAYTIPFYTP IPNGLYPSKS IMISGNVLPD ATRFHINLRC GGDIAFHLNP RFNENAVVRN TQINNSWGQE ERSLLGRMPF SRGQSFSVWI ICEGHCFKVA VNGQHMCEYY HRLKNLQDIN TLEVAGDIQL THVQT.
What applications can LGALS9 MOUSE Protein be used in?
LGALS9 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS9 MOUSE Protein?
The endotoxin level is minimal, LGALS9 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.
- View Data Sheet
Name :
IL 23 Human, HisDescription:
Interleukin-23 Human Recombinant, His Tag
Interleukin 23 alpha subunit p19, Interleukin-12 subunit beta p40, SGRF, IL23P19, IL-23-A, interleukin-six, G-CSF related factor, JKA3 induced upon T-cell activation, interleukin 12B (natural killer cell stimulatory factor 2 cytotoxic lymphocyte maturation factor 2 p40), NK cell stimulatory factor chain 2, Cytotoxic lymphocyte maturation factor 40 kDa subunit, CLMF2, CLMF p40.
Product # :
CYT-067Price :
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Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human Interleukin-23 produced in Sf9 Baculovirus cells is a glycosylated heterodimer composed of 2 disulfide-linked subunits. A p19 subunit which is unique to IL23 and a p40 subunit which is shared with IL12. The p19 subunit/IL23A (20-189aa, total of 176 aa, MW 19.5kDa) and p40 subunit /IL12B (23-328aa, total of 306 aa, MW 34.6kDa), the total predicted molecular mass of 54.1kDa (Molecular weight on SDS-PAGE will appear higher). IL23 is fused to a 6 aa His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL23 protein solution (1mg/ml) contains PBS (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Citations
More Info
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Introduction
IL23 is composed of a subunit of the heterodimeric cytokine IL23 and the p40 subunit of interleukin 12 (IL12B). Interleukin-23 (IL-23) belongs to the IL-12 family and is produced by antigen presenting cells. IL-23 using IL12RB1 and IL-23R (specific for IL-23) can activate STAT and NF-kB pathways and stimulate the production of interferon-gamma. ). IL-23 is known to take a vital part in the inflammation process and is associated with auto immune diseases. However, unlike IL12, which acts primarily on naive CD4(+) T cells, IL23 preferentially acts on memory CD4(+) T cells.
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Synonyms
Interleukin 23 alpha subunit p19, Interleukin-12 subunit beta p40, SGRF, IL23P19, IL-23-A, interleukin-six, G-CSF related factor, JKA3 induced upon T-cell activation, interleukin 12B (natural killer cell stimulatory factor 2 cytotoxic lymphocyte maturation factor 2 p40), NK cell stimulatory factor chain 2, Cytotoxic lymphocyte maturation factor 40 kDa subunit, CLMF2, CLMF p40.
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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
IL12B: IWELKKDVYV VELDWYPDAP GEMVVLTCDT PEEDGITWTL DQSSEVLGSG KTLTIQVKEF GDAGQYTCHK GGEVLSHSLL LLHKKEDGIW STDILKDQKE PKNKTFLRCE AKNYSGRFTC WWLTTISTDL TFSVKSSRGS SDPQGVTCGA ATLSAERVRG DNKEYEYSVE CQEDSACPAA EESLPIEVMV DAVHKLKYEN YTSSFFIRDI IKPDPPKNLQ LKPLKNSRQV EVSWEYPDTW STPHSYFSLT FCVQVQGKSK REKKDRVFTD KTSATVICRK NASISVRAQD RYYSSSWSEW ASVPCS.
IL23A: RAVPGGSSPA WTQCQQLSQK LCTLAWSAHP LVGHMDLREE GDEETTNDVP HIQCGDGCDP QGLRDNSQFC LQRIHQGLIF YEKLLGSDIF TGEPSLLPDS PVGQLHASLL GLSQLLQPEG HHWETQQIPS LSPSQPWQRL LLRFKILRSL QAFVAVAARV FAHGAATLSP HHHHHH.
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 :
TNFRSF17 HumanDescription:
B-Cell Maturation Antigen Human Recombinant
BCMA, CD269, Tumor Necrosis Factor Receptor Superfamily Member 17, BCM, TNFRSF17, B-cell maturation protein, CD269 antigen.
Product # :
CYT-598Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TNFRSF17 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 50 amino acids and having a molecular mass of 5.3 kDa. The TNFRSF17 is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
1mg of TNFRSF17 Human contain 20mM sodium phosphate buffer, pH-7.4, and 130mM NaCl.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
TNFRSF17 is a receptor for tnfsf13b/blys/baff and tnfsf13/april. TNFRSF17 promotes b-cell survival and plays a role in the regulation of humoral immunity. TNFRSF17 activates nf-kappa-b and jnk. TNFRSF17 is a member of the TNF-receptor superfamily. TNFRSF17 is expressed in mature B lymphocytes, and is invloved in B cell development and autoimmune response. TNFRSF17 specifically binds to the tumor TNFSF13B/TALL-1/BAFF, which causes NF-kappaB and MAPK8/JNK activation. TNFRSF17 binds to a variety of TRAF family members, and therefore transduces signals for cell survival and proliferation. TNFRSF17 is a type III membrane protein having 1 extracellular cysteine rich domain. Within the TNFRSF, it shares the highest homology with TACI. BCMA and TACI have both been shown to bind to APRIL and BAFF, members of the TNF ligand superfamily. BCMA expression has been found in immune organs. TNFRSF17 appears to be localized to the Golgi compartment. The binding of BCMA to APRIL or BAFF has been shown to stimulate IgM production in peripheral blood B cells and increase the survival of cultured B cells.
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Synonyms
BCMA, CD269, Tumor Necrosis Factor Receptor Superfamily Member 17, BCM, TNFRSF17, B-cell maturation protein, CD269 antigen.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TNFRSF17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNFRSF17 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 TNFRSF17 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
AGQCSQNEYF DSLLHACIPC QLRCSSNTPP LTCQRYCNAS VTNSVKGTNA.
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 :
M CSF MouseDescription:
Macrophage-Colony Stimulating Factor Mouse Recombinant
CSF-1, Lanimostim, MCSF, M-CSF.
Product # :
CYT-439Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Macrophage Colony Stimulating Factor Mouse Recombinant produced in E.coli is a disulfide linked homodimer, non-glycosylated, polypeptide chain containing 2 x 156 amino acids and having a total molecular mass of 36.4 KD.MCSF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a sterile (0.2µm) filtered solution containing 10mM sodium phosphate, 50mM sodium chloride, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as calculated by the dose-dependant stimulation of the proliferation of murine M-NFS-60 indicator cells is 1.33ng/ml corresponding to a specific activity of 7.5x105 units/mg.
Citations
More Info
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Introduction
Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.
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Synonyms
CSF-1, Lanimostim, MCSF, M-CSF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized M-CSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF 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 M-CSF 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
MKEVSEHCSH MIGNGHLKVL QQLIDSQMET SCQIAFEFVD QEQLDDPVCY LKKAFFLVQD IIDETMRFKD NTPNANATER LQELSNNLNS CFTKDYEEQN KACVRTFHET PLQLLEKIKN FFNETKNLLE KDWNIFTKNC NNSFAKCSSR DVVTKP.
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Background
Macrophage-Colony Stimulating Factor Mouse Recombinant: An In-Depth Analysis
Abstract:
Macrophage-Colony Stimulating Factor (M-CSF) is a crucial cytokine involved in the regulation of macrophage biology, including their differentiation, survival, and function. This research paper provides an in-depth analysis of M-CSF Mouse Recombinant, focusing on its structure, signaling pathways, and diverse functions in the context of human research. Additionally, the paper explores the therapeutic potential of M-CSF modulation in various diseases.
Introduction:
M-CSF plays a vital role in the development and maintenance of macrophages, key immune cells involved in innate immunity and tissue homeostasis. This paper aims to provide a comprehensive analysis of M-CSF Mouse Recombinant, highlighting its importance in human macrophage biology and its potential therapeutic applications.
Structure and Function of M-CSF:
M-CSF is a homodimeric protein that binds to its receptor, CSF-1R, leading to the activation of downstream signaling pathways. It regulates the proliferation, survival, and activation of macrophages, influencing immune responses and tissue remodeling processes.
Signaling Pathways:
Upon binding to CSF-1R, M-CSF triggers various intracellular signaling pathways, including the MAPK pathway, PI3K/Akt pathway, and JAK/STAT pathway. These pathways regulate gene expression and mediate cellular responses, impacting macrophage functions.
Role in Macrophage Development and Function:
M-CSF is essential for the differentiation and maturation of macrophages from hematopoietic progenitor cells. It promotes the survival, proliferation, and activation of macrophages, enhancing their phagocytic activity, cytokine production, and antigen presentation capabilities.
Therapeutic Potential:
Given its crucial role in macrophage biology, M-CSF modulation has emerged as a potential therapeutic strategy. M-CSF inhibitors and CSF-1R antagonists have shown promise in the treatment of inflammatory and autoimmune diseases, as well as certain cancers. Targeting M-CSF signaling can modulate immune responses and affect disease progression.
Clinical Applications and Future Directions:
The therapeutic potential of M-CSF modulation is being explored in various clinical settings. Clinical trials investigating M-CSF inhibitors as monotherapy or combination therapy are underway in diseases such as rheumatoid arthritis and cancer. Future research should focus on understanding the intricate mechanisms of M-CSF signaling, optimizing therapeutic strategies, and developing personalized treatment approaches.
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 :
HTF HumanDescription:
Holo Transferrin Human
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.
Product # :
PRO-315Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Holo Transferrin is a glycoprotein of approximately 77 kDa.
Source
Human serum.
Formulation
The protein (10mg/ml) was lyophilized from 20mM NH4HC03 solution.
May contain traces of buffer salts.Purity
Greater than 98.0% as determined by coomassie blue stained SDS-PAGE and Cellulose Acetate electrophoresis.
Citations
More Info
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Introduction
Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells. -
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.
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Physical Appearance
Sterile Filtered Pink lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized Holo Transferrin between 2-8°C, do not freeze. Upon reconstitution Apo Transferrin 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 Holo Transferrin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Human Virus Test
FDA approved Plasma from each donor has been tested and found negative for antibodies to HIV-1 & 2, HCV, HBsAG, HBc, HBV, HAV, HIV and Syphilis.
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Iron Content
The Iron content was estimated by ICP and was found to be 1232 ppm.
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.