Search results
570 results found for “Leukocyte Cell Derived Chemotaxin”
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Name :
TSLP HumanDescription:
Thymic Stromal Lymphopoietin Human Recombinant
Thymic Stromal Lymphopoietin, TSLP.
Product # :
CYT-572Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TSLP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids and having a molecular mass of 15 kDa.The TSLP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated solution (1mg/ml) contains 130mM NaCl, and 20mM sodium phosphate, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 is determined by the ability to induce proliferation of human Interleukin-7 receptor alpha & human TSLP Receptor co-transfected with mouse BaF3 cells which was found to be less than 0.3ng/ml.More Info
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Introduction
TSLP protein is a hemopoietic cytokine which signals throughout a heterodimeric receptor complex composed of the thymic stromal lymphopoietin receptor & the Interleukin-7 receptor alpha chain. TSLP impacts myeloid cells thus induces the discharge of T cell-attracting chemokines from monocytes & increases the growth of CD11c(+) dendritic cells. TSLP is mainly expressed in the heart, liver and prostate. TSLP is related in its biological activities with IL-7 and binds with the heterodimeric receptor complex consisting of the Interleukin-7 receptor alpha chain & the TSLPR. Similar to IL-7, TSLP enhances phosphorylation of STAT3 and STAT5, though uses kinases excluding JAKs for its activation. TSLP induces the release of T cell-attracting chemokines such asTARC & MDC from monocytes & triggers CD11c(+) dendritic cells. TSLP activated dendritic cells primes naive T cells to manufacture pro-allergic cytokines such as Iinterleukin-4, Interleukin-5, Interleukin-13 and TNF-alpha whereas down-regulating Interleukin-10 and IFN-gamma play a role in the initiation of allergic inflammation.
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Synonyms
Thymic Stromal Lymphopoietin, TSLP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TSLP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TSLP 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 TSLP 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
MYDFTNCDFE KIKAAYLSTI SKDLITYMSG TKSTEFNNTV SCSNRPHCLT EIQSLTFNPT AGCASLAKEM FAMKTKAALA IWCPGYSETQ INATQAMKKR RKRKVTTNKC LEQVSQLQGL WRRFNRPLLK QQ.
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 :
SIVA1 HumanDescription:
SIVA1 Human Recombinant
Apoptosis regulatory protein Siva isoform 1, Apoptosis regulatory protein Siva, CD27-binding protein, CD27BP, SIVA, SIVA1, Siva-1, Siva-2
Product # :
PRO-2652Price :
Quantity :
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Shipped with Ice Packs
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Description
SIVA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids (1-175 a.a.) and having a molecular mass of 21.1 kDa. SIVA1 is fused to a 23 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SIVA1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
SIVA1, also referred to asApoptosis regulatory protein Siva isoform 1, is a death domain-containing proapoptotic protein. It is known as glucocorticoid-induced TNFR family-related gene, and also as an intracellular ligand of CD27, which are both members of the TNFR family expressed on lymphoid cells. There isn’t much known about the signalling pathway underlying the Siva-induced apoptosis.SIVA1 expression is modulated in multiple pathological processes.
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Synonyms
Apoptosis regulatory protein Siva isoform 1, Apoptosis regulatory protein Siva, CD27-binding protein, CD27BP, SIVA, SIVA1, Siva-1, Siva-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 MGSMPKRSCP FADVAPLQLK VRVSQRELSR GVCAERYSQE VFEKTKRLLF LGAQAYLDHV WDEGCAVVHL PESPKPGPTG APRAARGQML IGPDGRLIRS LGQASEADPS GVASIACSSC VRAVDGKAVC GQCERALCGQ CVRTCWGCGS VACTLCGLVD CSDMYEKVLC TSCAMFET
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 12 p35 HumanDescription:
Interleukin-12 p35 Human Recombinant
NKSF1, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 35 kDa subunit (CLMF p35), TSF, Edodekin-alpha, IL-12 p35, IL-12A, IL-12 subunit p35, NK cell stimulatory factor chain 1, SGT2, FLJ39002.
Product # :
CYT-487Price :
Quantity :
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Shipped with Ice Packs
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Description
Interleukin-12 p35 His Human Recombinant produced in E.Coli is single, a non-glycosylated, polypeptide chain containing 197 amino acids fragment (57-253) with an amino-terminal hexahistidine tag. The IL-12 p35 His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Interleukin-12 p35 His-Tag is supplied in 1xPBS and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Active IL-12 is a p70 disulphide-linked dimer composed of p35 and p40 subunits. The protein is a pleiotropic cytokine produced primarily by antigen presenting cells and has multiple effects on T lymphocytes and natural killer cells in terms of stimulating cytotoxicity, proliferation, production of other cytokines and Th1 subset differentiation.
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Synonyms
NKSF1, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 35 kDa subunit (CLMF p35), TSF, Edodekin-alpha, IL-12 p35, IL-12A, IL-12 subunit p35, NK cell stimulatory factor chain 1, SGT2, FLJ39002.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
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 :
LGALS3 Mouse, ActiveDescription:
Galectin-3 Mouse Recombinant, BioActive
Lectin galactose binding soluble 3, Lectin, galactose binding, soluble 3, CBP35, GAL3, GALBP, GALIG, LGALS2, MAC2.
Product # :
CYT-1151Price :
Quantity :
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Shipped with Ice Packs
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- sds-page
Description
LGALS3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 287 amino acids ( 1-264 a.a) and having a molecular mass of 29.8kDa.LGALS3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
LGALS3 protein (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol,1mM DTT and 2mM EDTA.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Measured by its ability to agglutinate human red blood cells. The ED50 for this effect is ≥ 25ug/ml.
sds-page
More Info
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Introduction
Galectin 3, or LGALS3, is a protein which belongs to the animal lectins family, that binds betagalactoside residues selectively. LGALS3 is originated and leaves cells through ectocytosis. The protein is capable of inhibition apoptosis and the development of cancer. Galectin 3 is found in epithelial tissues in organisms, it can be located in dendritic cells, Kupffer cells, macrophages etc. LGALS3 levels elevated when inflammation is generating, cell proliferation, trans-activation by viral proteins and cell differentiation.
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Synonyms
Lectin galactose binding soluble 3, Lectin, galactose binding, soluble 3, CBP35, GAL3, GALBP, GALIG, LGALS2, MAC2.
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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 MGSMADSFSL NDALAGSGNP NPQGYPGAWG NQPGAGGYPG AAYPGAYPGQ APPGAYPGQA PPGAYPGQAP PSAYPGPTAP GAYPGPTAPG AYPGSTAPGA FPGQPGAPGA YPSAPGGYPA AGPYGVPAGP LTVPYDLPLP GGVMPRMLIT IMGTVKPNAN RIVLDFRRGN DVAFHFNPRF NENNRRVIVC NTKQDNNWGK EERQSAFPFE SGKPFKIQVL VEADHFKVAV NDAHLLQYNH RMKNLREISQ LGISGDITLT SANHAMI.
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Background
What is the molecular weight/Mw of LGALS3 MOUSE Protein?
LGALS3 MOUSE Protein has a total Mw of 29.8kDa.
What is the source or expression system of LGALS3 MOUSE Protein?
Escherichia Coli.
What is the Purity of LGALS3 MOUSE Protein?
LGALS3 MOUSE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS3 MOUSE Protein?
Measured by its ability to agglutinate human red blood cells. The ED50 for this effect is ≥ 25ug/ml.
What is the amino acid sequence of LGALS3 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMADSFSL NDALAGSGNP NPQGYPGAWG NQPGAGGYPG AAYPGAYPGQ APPGAYPGQA PPGAYPGQAP PSAYPGPTAP GAYPGPTAPG AYPGSTAPGA FPGQPGAPGA YPSAPGGYPA AGPYGVPAGP LTVPYDLPLP GGVMPRMLIT IMGTVKPNAN RIVLDFRRGN DVAFHFNPRF NENNRRVIVC NTKQDNNWGK EERQSAFPFE SGKPFKIQVL VEADHFKVAV NDAHLLQYNH RMKNLREISQ LGISGDITLT SANHAMI.
What applications can LGALS3 MOUSE Protein be used in?
LGALS3 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
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 :
KLRD1 AntibodyDescription:
Mouse Anti Human Killer Cell Lectin Like Receptor D1
Killer Cell Lectin Like Receptor D1, Killer Cell Lectin-Like Receptor Subfamily D, Member 1, NK Cell Receptor, CD94 Antigen, CD94, KP43, Killer Cell Lectin-Like Receptor Subfamily D Member 1, Natural Killer Cells Antigen CD94, KLRD1.
Product # :
ANT-717Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
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Introduction
KLRD1, also known as Killer Cell Lectin Like Receptor D1, is expressed on the surface of natural killer cells in the innate immune system. KLRD1 functions as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells. KLRD1 can create disulfide-bonded heterodimer with NKG2 family members. CD94 & NKG2 complex interacts with (HLA)-E, Human Leukocyte Antigen on target cells on the surface of natural killer cells.
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Synonyms
Killer Cell Lectin Like Receptor D1, Killer Cell Lectin-Like Receptor Subfamily D, Member 1, NK Cell Receptor, CD94 Antigen, CD94, KP43, Killer Cell Lectin-Like Receptor Subfamily D Member 1, Natural Killer Cells Antigen CD94, KLRD1.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human KLRD1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human KLRD1 protein 32-279 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and k light chain.
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Clone
PAT13E3AT.
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Applications
KLRD1 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
KLRD1 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
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 7 MouseDescription:
Interleukin-7 Mouse Recombinant
Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.
Product # :
CYT-372Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Interleukin-7 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 129 amino acids and having a molecular mass of 14.9kDa.
Source
Escherichia Coli.
Formulation
Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 1×PBS, pH7.4 and 2% trehalose.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50was determined by the dose-dependent stimulation of the proliferation of murine 2E8 cells is less than 0.2 ng/ml, corresponding to a specific activity of >5.0×106 IU/mg.More Info
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Introduction
Interleukin-7 is a potent lymphoid cell growth factor produced primarily by stromal cells. IL-7 has been shown to support the proliferation and differentiation of pre B- and early T cells as well as displaying a biological effect on cells of NK and myeloid lineages.
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Synonyms
Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL7 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 Interleukin 7 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
ECHIKDKEGK AYESVLMISI DELDKMTGTD SNCPNNEPNF FRKHVCDDTK EAAFLNRAAR KLKQFLKMNI SEEFNVHLLT VSQGTQTLVN CTSKEEKNVK EQKKNDACFL KRLLREIKTC WNKILKGSI.
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 :
KLRG1 HumanDescription:
Killer Cell Lectin-like Receptor Subfamily G, Member 1 Human Recombinant
Killer cell lectin-like receptor subfamily G member 1, C-type lectin domain family 15 member A, ITIM-containing receptor MAFA-L, MAFA-like receptor, Mast cell function-associated antigen, KLRG1, CLEC15A, MAFA, MAFAL, 2F1, MAFA-L, MAFA-2F1, MAFA-LIKE.
Product # :
PRO-1344Price :
Quantity :
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Shipped with Ice Packs
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Description
KLRG1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids (60-189 a.a) and having a molecular mass of 17kDa.KLRG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
KLRG1 protein solution (0.5mg/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.
More Info
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Introduction
Killer Cell Lectin-like Receptor Subfamily G, Member 1 (KLRG1) is a member of the killer cell lectin-like receptor (KLR) family, which is a group of transmembrane proteins preferentially expressed in NK cells. Natural killer (NK) cells are lymphocytes which mediate lysis of certain tumor cells and virus-infected cells without previous activation. NK cells can also regulate specific humoral and cell-mediated immunity. The cell surface expression of KLRG1 is up-regulated by MHC class I molecules expression.
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Synonyms
Killer cell lectin-like receptor subfamily G member 1, C-type lectin domain family 15 member A, ITIM-containing receptor MAFA-L, MAFA-like receptor, Mast cell function-associated antigen, KLRG1, CLEC15A, MAFA, MAFAL, 2F1, MAFA-L, MAFA-2F1, MAFA-LIKE.
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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 MGSLCQGSNY STCASCPSCP DRWMKYGNHC YYFSVEEKDW NSSLEFCLAR DSHLLVITDN QEMSLLQVFL SEAFCWIGLR NNSGWRWEDG SPLNFSRISS NSFVQTCGAI NKNGLQASSC EVPLHWVCKK VRL.
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 :
CTHRC1 Human, HEKDescription:
Collagen Triple Helix Repeat Containing 1 Human Recombinant, HEK
Collagen Triple Helix Repeat Containing 1, Protein NMTC1, CTHRC1.
Product # :
PRO-2028Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CTHRC1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Ser31-Lys243) containing a total of 219 amino acids, having a calculated molecular mass of 23.9kDa and fused to a 6 aa His tag at C-Terminus.
Source
HEK 293.
Formulation
CTHRC1 was filtered (0.4µm) and lyophilized in phosphate buffered saline pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Collagen triple helix repeat-containing protein 1 (CTHRC1) functions as a negative regulator of collagen matrix deposition. CTHRC1 is a secreted 28kDa protein which is glycosylated and highly conserved from lower chordates to mammals. CTHRC1 is highly connected with calcified tissues and cartilaginous matrix, but not with endothelial cells. CTHRC1 is detected qualitatively in plasma of healthy human subjects. CTHRC1 plasma levels are also significantly elevated during pregnancy, in diabetes, in inflammatory and infectious conditions, in subjects with acute myeloid leukemia but not in subjects with solid cancers. The hormonal functions of CTHRC1 include regulation of lipid storage and cellular glycogen levels with potentially far-reaching implications for cell metabolism and physiology. CTHRC1 gene deletion leads to fatty liver (steatosis) formation in mice while others exhibited inactivation of the CTHRC1 gene also results in low bone mass.
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Synonyms
Collagen Triple Helix Repeat Containing 1, Protein NMTC1, CTHRC1.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. CTHRC1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
SEIPKGKQKA QLRQREVVDL YNGMCLQGPA GVPGRDGSPG ANGIPGTPGI PGRDGFKGEK GECLRESFEE SWTPNYKQCS WSSLNYGIDL GKIAECTFTK MRSNSALRVL FSGSLRLKCR NACCQRWYFT FNGAECSGPL PIEAIIYLDQ GSPEMNSTIN IHRTSSVEGL CEGIGAGLVD VAIWVGTCSD YPKGDASTGW NSVSRIIIEE LPK 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 :
SCF RatDescription:
Stem Cell Factor Rat Recombinant
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250, Hematopoietic growth factor KL.
Product # :
CYT-323Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Stem cell factor Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (26-189) and having a molecular mass of 18.4 kDa.The Rat SCF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 is determined by the dose-dependant stimulation of the proliferation of human TF-1 cells which is < 10 ng/ml, corresponding to a specific activity of 100,000units/mg.More Info
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Introduction
Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117 (c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases.
SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid). -
Synonyms
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250, Hematopoietic growth factor KL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized rat SCF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCF 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 SCF 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
MQEICRNPVT DNVKDITKLV ANLPNDYMIT LNYVAGMDVL PSHCWLRDMV THLSVSLTTL LDKFSNISEG LSNYSIIDKL GKIVDDLVAC MEENAPKNVK ESLKKPETRN FTPEEFFSIF NRSIDAFKDF MVASDTSDCV LSSTLGPEKD SRVSVTKPFM LPPVA.
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 :
CD226 HumanDescription:
CD226 Human Recombinant
DNAM-1, PTA1, TLiSA1, CD226 antigen, DNAX accessory molecule 1, DNAM1, Recombinant Human CD226.
Product # :
PRO-1353Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CD226 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 259 amino acids (19-254a.a.) and having a molecular mass of 29.4kDa.CD226 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CD226 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
CD226 belongs to the Ig-superfamily containing 2 Ig-like domains of the V-set. CD226 is a 65kDa glycoprotein expressed on the surface NK cells, platelets, monocytes and a subset of T cells. CD226 facilitates cellular adhesion of platelets and megakaryocytic cells to vascular endothelial cells. CD226 also plays a role in megakaryocytic cell maturation.
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Synonyms
DNAM-1, PTA1, TLiSA1, CD226 antigen, DNAX accessory molecule 1, DNAM1, Recombinant Human CD226.
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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 MGSEEVLWHT SVPFAENMSL ECVYPSMGIL TQVEWFKIGT QQDSIAIFSP THGMVIRKPY AERVYFLNST MASNNMTLFF RNASEDDVGY YSCSLYTYPQ GTWQKVIQVV QSDSFEAAVP SNSHIVSEPG KNVTLTCQPQ MTWPVQAVRW EKIQPRQIDL LTYCNLVHGR NFTSKFPRQI VSNCSHGRWS VIVIPDVTVS DSGLYRCYLQ ASAGENETFV MRLTVAEGKT DNQYTLFVA.
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 :
Betacellulin HumanDescription:
Betacellulin Human Recombinant
Product # :
CYT-330Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Betacellulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 80 amino acids and having a molecular mass of 9 kDa. Betacellulin Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Betacellulin Human Recombinant was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 0.05 ng/ml. corresponding to a Specific Activity of >20,000,000IU/mg.More Info
-
Introduction
Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Betacellulin Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BTC Human 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 BTC Human in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY
-
Background
Betacellulin Human Recombinant: Illuminating Pathways in Regenerative Medicine
Introduction
In the ever-evolving landscape of regenerative medicine, a promising new chapter unfolds with the arrival of Betacellulin Human Recombinant (BTC). This growth factor holds tremendous potential, offering a glimpse into the future of transformative therapeutic interventions.
BTC: The Architect of Cellular Revitalization
BTC, a member of the EGF family, has long been recognized for its pivotal role in cellular proliferation and differentiation. The emergence of BTC in its recombinant form has sparked excitement, igniting new possibilities for regenerative medicine.
Crafting the Alchemist: Pioneering Methodologies
Through the adept utilization of biotechnological techniques, we successfully synthesized BTC human recombinant. Our meticulous in vitro investigations delved into BTC's capacity to orchestrate intricate cellular processes, paving the way for therapeutic advancements.
Unveiling the Biological Tapestry
Buoyed by encouraging in vitro findings, we embarked on in vivo studies utilizing animal models. This natural setting allowed us to witness BTC human recombinant's impact within a living organism, unraveling the intricate nuances of its regenerative potential.
A Flourish of Results
The journey from laboratory to living system yielded promising results. BTC human recombinant showcased a significant influence on cellular proliferation and differentiation, underscoring its role as a key player in tissue regeneration and regenerative therapies.
Charting a Transformative Future
As the story of BTC human recombinant unfolds, it beckons further exploration through extensive human-centric clinical trials. These trials will serve as a compass, guiding us towards harnessing the full therapeutic potential of BTC, ushering in a new era of healing and regeneration.
What is the molecular weight/Mw of BTC Protein?
BTC Protein has a total Mw of 9kDa.
What is the source or expression system of BTC Protein?
Escherichia Coli.
What is the Purity of BTC Protein?
BTC Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of BTC Protein?
The ED50, calculated by the dose-dependant proliferation of murine BALB\C 3T3 cells (measured by 3H-thymidine uptake) is < 0.05 ng/ml. corresponding to a Specific Activity of >20,000,000IU/mg.
What is the amino acid sequence of BTC Protein?
DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY
What applications can BTC Protein be used in?
BTC Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BTC Protein?
The endotoxin level is minimal, BTC 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 :
Betacellulin MouseDescription:
Betacellulin Mouse Recombinant
Betacellulin, Probetacellulin.
Product # :
CYT-131Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
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- More Info
Description
BTC Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 80 amino acids and having a molecular mass of 9.0kDa. The BTC is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1×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 was determined by the dose-dependent stimulation of the proliferation of mouse Balb/3T3 cells is < 0.01 ng/ml, corresponding to a Specific Activity of > 1.0×108 IU/mg.
More Info
-
Introduction
BTC is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.
-
Synonyms
Betacellulin, Probetacellulin.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized BTC although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BTC 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 BTC Mouse Recombinant in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
DGNTTRTPET NGSLCGAPGE NCTGTTPRQK VKTHFSRCPK QYKHYCIHGR CRFVVDEQTP SCICEKGYFG ARCERVDLFY
-
Background
What is the molecular weight/Mw of BETACELLULIN Protein?
BETACELLULIN Protein has a total Mw of 9kDa.
What is the source or expression system of BETACELLULIN Protein?
Escherichia Coli.
What is the Purity of BETACELLULIN Protein?
BETACELLULIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BETACELLULIN Protein?
The ED50 was determined by the dose-dependent stimulation of the proliferation of mouse Balb/3T3 cells is < 0.01 ng/ml, corresponding to a Specific Activity of > 1.0×108 IU/mg.
What is the amino acid sequence of BETACELLULIN Protein?
DGNTTRTPET NGSLCGAPGE NCTGTTPRQK VKTHFSRCPK QYKHYCIHGR CRFVVDEQTP SCICEKGYFG ARCERVDLFY
What applications can BETACELLULIN Protein be used in?
BETACELLULIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BETACELLULIN Protein?
The endotoxin level is minimal, BETACELLULIN 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 :
CD80 HumanDescription:
CD80 Human Recombinant
CD80 Molecule, CD80 Antigen (CD28 Antigen Ligand 1, B7-1 Antigen), B-Lymphocyte Activation Antigen B7, CTLA-4 Counter-Receptor B7.1, Activation B7-1 Antigen, CD28LG1, CD28LG, LAB7, BB1, B7, Costimulatory Molecule Variant IgV-CD80, T-Lymphocyte Activation Antigen CD80, Costimulatory Factor CD80, CD80 Antigen, B7-1, B7.1.
Product # :
PRO-2473Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CD80 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 216 amino acids (35-242a.a.) and having a molecular mass of 24.9kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).CD80 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
CD80 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
CD80 which is a member of cell surface immunoglobulin superfamily takes part in the costimulatory signal essential for T-lymphocyte activation. CD80 binds to either human or mouse CD28 and CTLA-4 – binding to CD28 induces T-cell proliferation and cytokine production while binding to CTLA-4 inhibits T-cell activation. CD80 is expressed on activated B cells, activated T cells, and macrophages.
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Synonyms
CD80 Molecule, CD80 Antigen (CD28 Antigen Ligand 1, B7-1 Antigen), B-Lymphocyte Activation Antigen B7, CTLA-4 Counter-Receptor B7.1, Activation B7-1 Antigen, CD28LG1, CD28LG, LAB7, BB1, B7, Costimulatory Molecule Variant IgV-CD80, T-Lymphocyte Activation Antigen CD80, Costimulatory Factor CD80, CD80 Antigen, B7-1, B7.1.
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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.
-
Amino Acid Sequence
VIHVTKEVKE VATLSCGHNV SVEELAQTRI YWQKEKKMVL TMMSGDMNIW PEYKNRTIFD ITNNLSIVIL ALRPSDEGTY ECVVLKYEKD AFKREHLAEV TLSVKADFPT PSISDFEIPT SNIRRIICST SGGFPEPHLS WLENGEELNA INTTVSQDPE TELYAVSSKL DFNMTTNHSF MCLIKYGHLR VNQTFNWNTT KQEHFPDNLE 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.
- View Data Sheet
Name :
CEA HumanDescription:
Carcinoembryonic Antigen Human Recombinant
CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.
Product # :
PRO-287Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CEA Human Recombinant is glycosylated with N-linked sugars and produced using baculovirus vectors in insect cells. CEA is a well-known tumor marker corresponding to the full length human CEA which is approximately 120,000 Dalton.
Source
Baculovirus Insect Cells.
Formulation
The sterile protein solution contains 10mM NaH2PO4, pH 7 and 150mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Carcinoembryonic antigen (CEA) is a glycoprotein present in fetal digestive-tract tissues; it’s involved in cell adhesion. The production of CEA stops before birth. CEA is called tumor marker since its elevated levels are found in the serum from individuals with colorectal, gastric, pancreatic, lung and breast carcinomas and in heavy smokers.
There are also benign conditions that elevate CEA levels such as smoking, infection, inflammatory bowel disease, pancreatitis, cirrhosis of the liver, and some benign tumors (in the equivalent organs which have cancers with elevated CEA). Typically, higher levels of CEA are found in men, smokers, and older individuals.
The presence of CEA assists in screening, in evaluating recurrent or disseminated disease, and in determining the success of surgical removal of malignant tumors.
CEA levels can be used as indicators of treatment success. The normal values range from 0.0 to 2.5 ng/ml of serum (from blood), in non-smokers, a greater amount than that may be suggestive of cancer. Levels above 20 ng/ml before treatment are associated with cancer which has already metastasized. Benign conditions do not usually cause a CEA increase over 10 ng/ml.
The high levels of CEA should return to normal after successful therapy, however if during follow up there’s an elevation in CEA levels it indicates a recurrence of tumor.
Carcinoembryonic antigen family belongs to the immunoglobulin superfamily; it consists of 29 genes, 18 of which are normally expressed. -
Synonyms
CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.
-
Physical Appearance
Sterile Filtered colourless solution.
-
Stability
CEA should be stored at 2-8°C.Avoid freezing.
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 :
TAFA2 HumanDescription:
Family with Sequence Similarity 19 Member A2 Human Recombinant
Family with sequence similarity 19 (chemokine (C-C motif)-like) member A2, Chemokine-like protein TAFA-2, protein FAM19A2.
Product # :
CYT-118Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
- purity
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Description
TAFA2 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 101 amino acids and having a molecular mass of 11.2kDa. The TAFA2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH7.4.
Purity
Greater than 97.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Fully biologically active when compared to standard. Measured by its ability to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons.More Info
-
Introduction
TAFA-2 is a 11 kDa secreted protein that belongs to the FAM19/TAFA family of chemokine-like proteins. Similar to other FAM19/TAFA family members, mature TAFA-1 contains 10 regularly spaced cysteine residues with the same pattern: CX7CCX13CXCX14CX11CX4CX5CX10C (C symbolizes a conserved cysteine residue and X symbolizes any noncysteine amino acid). Human TAFA-2 is 97% aa identical to mouse TAFA-2 and is expressed in the central nervous system (CNS), colon, heart, lung, spleen, kidney, and thymus, however its expression in the CNS is 50 to 1000 fold higher than in other tissues. The biological roles of TAFA family members have not yet been determined.
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Synonyms
Family with sequence similarity 19 (chemokine (C-C motif)-like) member A2, Chemokine-like protein TAFA-2, protein FAM19A2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized TAFA2 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TAFA2 should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized TAFA2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
ANHHKAHHVK TGTCEVVALH RCCNKNKIEE RSQTVKCSCF PGQVAGTTRA APSCVDASIV EQKWWCHMQP CLEGEECKVL PDRKGWSCSS GNKVKTTRVT H
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GM-CSF Poricne, HisDescription:
Granulocyte Macrophage-Colony Stimulating Factor Porcine Recombinant, His Tag
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim
Product # :
CYT-1160Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
GMCSF Poricne Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 148 amino acids (18-144a.a.) and having a molecular mass of 16.6kDa.GMCSF is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GMCSF protein solution (0.5mg/ml) containing Phosphate-Buffered Saline (pH7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range is ≤ 40 ng/ml, and is measured in a cell proliferation assay using TF-1 human erythroleukemic cells.
More Info
-
Introduction
The hematopoietic growth factor GM-CSF or granulocyte macrophage colony-stimulating factor, stimulates the development of neutrophils & macrophages, enhance proliferation and development of early erythroid megakaryocytic & eosinophilic progenitor cells. GM-CSF is secreted from the fibroblasts, monocytes, T-lymphocytes & endothelial cells. This protein blocks the migration of neutrophils & induces the biological activity of mature end-cells.
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Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim
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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 MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK
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Background
What is the molecular weight/Mw of GM-CSF PORCINE, HIS Protein?
GM-CSF PORCINE, HIS Protein has a total Mw of 16.6kDa.
What is the source or expression system of GM-CSF PORCINE, HIS Protein?
Escherichia Coli.
What is the Purity of GM-CSF PORCINE, HIS Protein?
GM-CSF PORCINE, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GM-CSF PORCINE, HIS Protein?
The ED50 range is ≤ 40 ng/ml, and is measured in a cell proliferation assay using TF-1 human erythroleukemic cells.
What is the amino acid sequence of GM-CSF PORCINE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MAPTRPPSPV TRPWQHVDAI KEALSLLNNS NDTAAVMNET VDVVCEMFDP QEPTCVQTRL NLYKQGLRGS LTRLKSPLTL LAKHYEQHCP LTEETSCETQ SITFKSFKDS LNKFLFTIPF DCWGPVKK
What applications can GM-CSF PORCINE, HIS Protein be used in?
GM-CSF PORCINE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GM-CSF PORCINE, HIS Protein?
The endotoxin level is minimal, GM-CSF PORCINE, 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.
- View Data Sheet
Name :
CD100 Human HEKDescription:
CD100 Human Recombinant HEK
Thesemaphorin family containing 1 Ig-like C2-type domain, 1 PSI domain and 1 Sema domai,Semaphorin-4D, A8, BB18, GR3, SEMA4D, C9orf164, CD100, SEMAJ.
Product # :
PRO-1640Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- purity
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Description
CD100 Human Recombinant produced by mammalian expression system in human cells is a single polypeptide chain containing 721 amino acids (22-734). CD100 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
CD100 was lyophilized from a 0.2 µM filtered solution of 20mM PB and 150mM NaCl, PH 7.4.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Semaphorin-4D (CD100) is a member of the semaphorin family containing 1 Ig-like C2-type domain, 1 PSI domain and 1 Sema domain. CD100 is the cell surface receptor forPLXN1B and PLXNB2 which plays a central role in cell-cell signaling. CD100 stimulates the migration of cerebellar granule cells and of endothelial cells, regulates dendrite and axon branching and morphogenesis. In addition, CD100 has a role in the immune system; it promotes signaling via SRC and PTK2B/PYK2, which subsequently mediates activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade.
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Synonyms
Thesemaphorin family containing 1 Ig-like C2-type domain, 1 PSI domain and 1 Sema domai,Semaphorin-4D, A8, BB18, GR3, SEMA4D, C9orf164, CD100, SEMAJ.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized CD100 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CD100 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized CCD100 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MAFAPIPRITWEHREVHLVQFHEPDIYNYSALLLSEDKDTLYIGAREAVFAVNALNISEKQHE
VYWKVSEDKKAKCAEKGKSKQTECLNYIRVLQPLSATSLYVCGTNAFQPACDHLNLTSFKFLG
KNEDGKGRCPFDPAHSYTSVMVDGELYSGTSYNFLGSEPIISRNSSHSPLRTEYAIPWLNEPSF
VFADVIRKSPDSPDGEDDRVYFFFTEVSVEYEFVFRVLIPRIARVCKGDQGGLRTLQKKWTSFL
KARLICSRPDSGLVFNVLRDVFVLRSPGLKVPVFYALFTPQLNNVGLSAVCAYNLSTAEEVFSH
GKYMQSTTVEQSHTKWVRYNGPVPKPRPGACIDSEARAANYTSSLNLPDKTLQFVKDHPLMDDSV
TPIDNRPRLIKKDVNYTQIVVDRTQALDGTVYDVMFVSTDRGALHKAISLEHAVHIIEETQLFQD
FEPVQTLLLSSKKGNRFVYAGSNSGVVQAPLAFCGKHGTCEDCVLARDPYCAWSPPTATCVALHQ
TESPSRGLIQEMSGDASVCPDKSKGSYRQHFFKHGGTAELKCSQKSNSEKTMYLKSSDNRVDHHHHHH.
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 :
DEFB116 HumanDescription:
Beta Defensin 116 Human Recombinant
Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.
Product # :
CYT-713Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- sds-page
Description
DEFB116 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 102 amino acids (24-102 a.a) and having a molecular mass of 11.5kDa.DEFB116 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DEFB116 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Beta Defensin 116, also known as DEFB116 is a member of the beta-defensin family.DEFB116 has antibacterial activity. The innate immune system includes antimicrobial peptides that protect multicellular organisms from a diverse spectrum of microorganisms. In addition, Beta-Defensins contain one important family of mammalian antimicrobial peptides.
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Synonyms
Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.
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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 MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.
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Background
Title: Beta Defensin 116 Human Recombinant: An Insight into its Antimicrobial Properties and Therapeutic Applications
Abstract:
Beta defensin 116 (BD116) is a key member of the beta defensin family, known for its potent antimicrobial activity against various pathogens. This research paper provides an in-depth analysis of human recombinant BD116, focusing on its production, characterization, and potential applications in antimicrobial therapy. The paper highlights the significance of BD116 in innate immunity and its role in combating microbial infections. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD116 in various infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD116 and its utility as a research tool and a potential antimicrobial agent.Introduction:
Beta defensin 116 (BD116) is a small cationic peptide that plays a crucial role in the innate immune response against microbial pathogens. Human recombinant BD116, produced through genetic engineering techniques, offers a valuable tool for studying its antimicrobial properties and exploring its therapeutic potential.Production and Characterization:
Recombinant BD116 is typically generated using expression systems such as bacteria or yeast. The protein is then purified and characterized to ensure its structural integrity and antimicrobial activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant BD116.Antimicrobial Properties:
BD116 exhibits broad-spectrum antimicrobial activity against bacteria, fungi, and viruses. It functions by disrupting the microbial cell membrane and interfering with essential cellular processes. Recombinant BD116 serves as a valuable tool for investigating the mechanisms underlying its antimicrobial action and exploring its potential as an antimicrobial agent.Therapeutic Implications:
The emergence of multidrug-resistant pathogens poses a significant challenge in the treatment of infectious diseases. Recombinant BD116 holds promise as an alternative therapeutic option due to its potent antimicrobial properties. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD116 in various infectious diseases, including bacterial skin infections and respiratory tract infections.Conclusion:
Human recombinant BD116 is a valuable research tool and a potential antimicrobial agent. Its production, characterization, and applications in antimicrobial therapy contribute to our understanding of innate immunity and the development of novel therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD116 offer promising prospects for combating multidrug-resistant pathogens and improving outcomes in infectious diseases.What is the molecular weight/Mw of DEFB116 Protein?
DEFB116 Protein has a total Mw of 11.5kDa.
What is the source or expression system of DEFB116 Protein?
Escherichia Coli.
What is the Purity of DEFB116 Protein?
DEFB116 Protein is >80% pure as determined by SDS-PAGE.
What is the Biological Activity of DEFB116 Protein?
The biological functionality of DEFB116 Protein will be determined in the future.
What is the amino acid sequence of DEFB116 Protein?
MGSSHHHHHH SSGLVPRGSH MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.
What applications can DEFB116 Protein be used in?
DEFB116 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for DEFB116 Protein?
The endotoxin level is minimal, DEFB116 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 16 Human, HisDescription:
Interleukin-16 Human Recombinant, His Tag
IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.
Product # :
CYT-562Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Interleukin-16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain (502-631 a.a) containing 150 amino acids and having a molecular mass of 15.5kDa. The IL-16 is fused to a 20 a.a His-Tag at N-Terminus.The IL-16 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL-16 His tag protein (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM PMSF & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
IL-16 is a pleiotropic cytokine that functions as a chemoattractant, a modulator of T cell activation, and an inhibitor of HIV replication. The signaling process of IL-16 is mediated by CD4. The product of this gene undergoes proteolytic processing, which is found to yield two functional proteins. IL-16 functions exclusively attributed to the secreted C-terminal peptide, while the N-terminal product may play a role in cell cycle control. Caspase 3 is reported to be involved in the proteolytic processing of this protein. Two transcript variants encoding different isoforms have been found for this gene.
IL-16 stimulates a migratory response in cd4+ lymphocytes, monocytes, and eosinophils. Also induces t-lymphocyte expression of interleukin 2 receptor, ligand for cd4. -
Synonyms
IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.
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Physical Appearance
Sterile Filtered solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPDLNSSTDS AASASAASDV SVESTAEATV CTVTLEKMSAGLGFSLEGGK GSLHGDKPLT INRIFKGAAS EQSETVQPGD EILQLGGTAM QGLTRFEAWN IIKALPDGPV TIVIRRKSLQ SKETTAAGDS.
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 :
TNFSF8 HumanDescription:
CD30 Ligand Human Recombinant
Tumor necrosis factor ligand superfamily member 8, CD30 ligand, CD30-L, CD153, TNFSF8, CD30L, CD30LG, CD30 Antigen Ligand, CD153 Antigen.
Product # :
CYT-824Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TNFSF8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids (63-234 a.a.) and having a molecular mass of 22kDa.TNFSF8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TNFSF8 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
CD30 Ligand (TNFSF8) is a cytokine which is a member of the tumor necrosis factor (TNF) ligand family. The TNFSF8 cytokine is a ligand for TNFRSF8/CD30, which is a cell surface antigen and a marker for Hodgkin lymphoma and related hematologic malignancies. The employment of the TNFSF8 cytokine expressed on B cell surface has an inhibitory role in modulating Ig class switch. TNFSF8 enhances cell proliferation of some lymphoma cell lines, while inducing cell death and reducing cell proliferation of other lymphoma cell lines. The pleiotropic biological activities of the TNFSF8 cytokine on different CD30+ lymphoma cell lines has a pathophysiologic role in Hodgkin's and some non-Hodgkin's lymphomas.
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Synonyms
Tumor necrosis factor ligand superfamily member 8, CD30 ligand, CD30-L, CD153, TNFSF8, CD30L, CD30LG, CD30 Antigen Ligand, CD153 Antigen.
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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 MGSQRTDSIP NSPDNVPLKG GNCSEDLLCI LKRAPFKKSW AYLQVAKHLN KTKLSWNKDG ILHGVRYQDG NLVIQFPGLY FIICQLQFLV QCPNNSVDLK LELLINKHIK KQALVTVCES GMQTKHVYQN LSQFLLDYLQ VNTTISVNVD TFQYIDTSTF PLENVLSIFL YSNSD.
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 9 MouseDescription:
Interleukin-9 Mouse Recombinant
P40, HP40, T-cell growth factor p40, IL-9, P40 cytokine.
Product # :
CYT-373Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Interleukin-9 Mouse Recombinant produced in E.Coli is a single, non-glycosylated single polypeptide chain containing 127 amino acids and having a molecular mass of 14.3kDa. The IL-9 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution 10mM Na2PO4, pH 7.5.
Purity
Greater than 96.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependant stimulation of human MO7e cells is < 0.5 ng/ml, corresponding to a Specific Activity of 2,000,000IU/mg.More Info
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Introduction
Factor that is thought to be a regulator of hematopoiesis. It has been shown to enhance the growth of human mast cells and megakaryoblastic leukemic cells as well as murine helper t-cell clones. IL-9 is a glycoprotein with a molecular weight of 32-39 that is derived from T-cells, and maps to human chromosome 5.
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Synonyms
P40, HP40, T-cell growth factor p40, IL-9, P40 cytokine.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-9 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL9 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 Interleukin 9 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
MQRCSTTWGI RDTNYLIENL KDDPPSKCSC SGNVTSCLCL SVPTDDCTTP CYREGLLQLT NATQKSRLLP VFHRVKRIVE VLKNITCPSF SCEKPCNQTM AGNTMSFLKS LLGTFQKTEM QRQKSRP.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.6 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-9 as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL 4 Human, YeastDescription:
Interleukin 4 Human Recombinant, Yeast
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
Product # :
CYT-712Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Interleukin-4 Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 129 amino acids.The IL-4 is purified by proprietary chromatographic techniques.
Source
Pichia pastoris.
Formulation
The protein was lyophilized from 0.2µm filtered solution in 20mM sodium phosphate buffer pH 6.0 in absence of any carrier protein.
Purity
Greater than 98% as determined by SDS-PAGE.
Biological Activity
The biological activity is determined by measuring the dose-dependent proliferation of human TF–1 cells and CD23 expression. A concentration range of 0.1–10.0 ng/ml is effective for most in vitro applications. ED50 = 0.05–0.4ng/ml.More Info
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Introduction
IL4 is a pleiotropic cytokine produced by activated T cells. IL4 is a ligand for interleukin 4 receptor. The interleukin 4 receptor also binds to IL13, which may contribute to many overlapping functions of this cytokine and IL13. STAT6, a signal transducer and activator of transcription, has been shown to play a central role in mediating the immune regulatory signal of this cytokine. This gene, IL3, IL5, IL13, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL13. IL4, IL13 and IL5 are found to be regulated coordinately by several long-range regulatory elements in an over 120 kilobase range on the chromosome. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.
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Synonyms
BCGF, BCDF, B cell stimulating factor, BSF-1, Lymphocyte stimulatory factor 1, IL-4, MGC79402, Binetrakin, Pitrakinra.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Interleukin-4 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 Interleukin-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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 :
IL6ST HumanDescription:
Interleukin-6 Signal Transducer Human Recombinant
Interleukin 6 signal transducer, oncostatin M receptor, IL6ST, CD130, CDw130, GP130, GP130-RAPS, IL6R-beta
Product # :
CYT-1156Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IL6ST Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 605 amino acids (23-619 a.a) and having a molecular mass of 68.9kDa.IL6ST is fused to an 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The IL6ST solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Interleukin-6 Signal Transducer or IL6ST is a receptor, part of the family of class 1 cytokine receptor. IL6ST binds to IL-6 through membrane-anchored or soluble IL-6R starts a connection between another complex of IL6ST and IL-6 , thus forming a homo-dimer and a signal transduction occurs.
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Synonyms
Interleukin 6 signal transducer, oncostatin M receptor, IL6ST, CD130, CDw130, GP130, GP130-RAPS, IL6R-beta
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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
ELLDPCGYIS PESPVVQLHS NFTAVCVLKE KCMDYFHVNA NYIVWKTNHF TIPKEQYTII NRTASSVTFT DIASLNIQLT CNILTFGQLE QNVYGITIIS GLPPEKPKNL SCIVNEGKKM RCEWDRGRET HLETNFTLKS EWATHKFADC KAKRDTPTSC TVDYSTVYFV NIEVWVEAEN ALGKVTSDHI NFDPVYKVKP NPPHNLSVIN SEELSSILKL TWTNPSIKSV IILKYNIQYR TKDASTWSQI PPEDTASTRS SFTVQDLKPF TEYVFRIRCM KEDGKGYWSD WSEEASGITY EDRPSKAPSF WYKIDPSHTQ GYRTVQLVWK TLPPFEANGK ILDYEVTLTR WKSHLQNYTV NATKLTVNLT NDRYVATLTV RNLVGKSDAA VLTIPACDFQ ATHPVMDLKA FPKDNMLWVE WTTPRESVKK YILEWCVLSD KAPCITDWQQ EDGTVHRTYL RGNLAESKCY LITVTPVYAD GPGSPESIKA YLKQAPPSKG PTVRTKKVGK NEAVLEWDQL PVDVQNGFIR NYTIFYRTII GNETAVNVDS SHTEYTLSSL TSDTLYMVRM AAYTDEGGKD GPEFTFTTPK FAQGEIELEH HHHHH
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Background
Significance of Human Recombinant Interleukin-6 Signal Transducer: Insights and Implications
Abstract:
The Interleukin-6 (IL-6) signal transducer holds a pivotal role in the complex IL-6 signaling pathway, orchestrating crucial cellular responses. This paper delves into the significance of Human Recombinant IL-6 Signal Transducer in unraveling IL-6-mediated cellular communication and highlights its potential applications in research and therapeutic development. The review sheds light on the methodology of producing this transducer and its relevance in advancing our understanding of cytokine signaling.
Introduction:
IL-6, a pleiotropic cytokine, is known to exert its diverse effects through a complex signaling cascade, wherein the signal transducer plays a crucial role. The availability of Human Recombinant IL-6 Signal Transducer enables the investigation of its role in health and disease. This transducer is vital for transmitting IL-6 signals, influencing processes like immune response, inflammation, and cell differentiation.
IL-6 Signal Transduction Pathway:
The IL-6 signal transduction pathway involves binding of IL-6 to its receptor, leading to the recruitment of the signal transducer and subsequent activation of downstream signaling molecules such as JAK/STAT pathway. This orchestrated response modulates gene expression, thereby impacting cellular behavior.
Methods of Production:
Human Recombinant IL-6 Signal Transducer is produced by expressing the corresponding gene in a suitable expression system, often utilizing bacterial or mammalian cells. Proper post-translational modifications are necessary to ensure its biological activity and appropriate functioning within the signaling cascade.
Applications in Research:
Human Recombinant IL-6 Signal Transducer serves as a fundamental tool in elucidating IL-6-mediated signaling mechanisms. Its availability facilitates the exploration of how aberrant signaling contributes to diseases such as autoimmune disorders, inflammatory conditions, and certain cancers. The transducer's interaction with other signaling pathways is also of interest for comprehensive pathway analysis.
Therapeutic Implications:
Understanding the IL-6 signal transduction pathway has led to the development of targeted therapies for IL-6-related diseases. Modulation of this pathway presents potential opportunities for novel therapeutic interventions, thereby offering a new dimension in precision medicine.
Challenges and Future Directions:
While the availability of Human Recombinant IL-6 Signal Transducer has significantly advanced our knowledge, challenges remain in deciphering the intricate nuances of IL-6 signaling. Developing strategies to selectively intervene in this pathway without disturbing physiological homeostasis presents an ongoing challenge.
Conclusion:
The Human Recombinant IL-6 Signal Transducer serves as a cornerstone in unraveling the complexities of IL-6 signaling, shedding light on its roles in health and disease. Its applications span from fundamental research to therapeutic development, showcasing its potential to shape the future of precision medicine.
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 Human, HisDescription:
B-Cell Maturation Antigen Human Recombinant, His Tag
BCMA, CD269, Tumor Necrosis Factor Receptor Superfamily Member 17, BCM, TNFRSF17, B-cell maturation protein, CD269 antigen.
Product # :
CYT-190Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TNFRSF17 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (78-184 a.a) and having a molecular mass of 14.1kDa.TNFRSF17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TNFRSF17 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
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 colorless liquid.
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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 MGSRKINSEP LKDEFKNTGS GLLGMANIDL EKSRTGDEII LPRGLEYTVE ECTCEDCIKS KPKVDSDHCF PLPAMEEGAT ILVTTKTNDY CKSLPAALSA TEIEKSISAR.
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.