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Name :
SYT13 HumanDescription:
Synaptotagmin XIII Human Recombinant
Synaptotagmin XIII, KIAA1427, synaptotagmin-13, sytXIII.
Product # :
PRO-1550Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SYT13 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 420 amino acids (30-426) and having a molecular mass of 46.5kDa.SYT13 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SYT13 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT, 1mM PMSF, 1mM EDTA and 30% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
SYT13 belongs to the great synaptotagmin protein family which contain 2 domains: cytoplasmic C terminus with two tandem C2 domains (C2A and C2B) and extracellular N-terminal transmembrane domain. Synaptotogmin family members have dissimilar biochemical properties and developmental profiles, and patterns of tissue distribution. Additionally, Synaptotogmins formulate homo- and heteromeric complexes with each other. Synaptotagmins operate as membrane traffickers in multicellular organisms.
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Synonyms
Synaptotagmin XIII, KIAA1427, synaptotagmin-13, sytXIII.
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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 MGSCRHMHPK KGLLPRDQDP DLEKAKPSLL GSAQQFNVKK STEPVQPRAL LKFPDIYGPR PAVTAPEVIN YADYSLRSTE EPTAPASPQP PNDSRLKRQV TEELFILPQN GVVEDVCVME TWNPEKAASW NQAPKLHYCL DYDCQKAELF VTRLEAVTSN HDGGCDCYVQ GSVANRTGSV EAQTALKKRQ LHTTWEEGLV LPLAEEELPT ATLTLTLRTC DRFSRHSVAG ELRLGLDGTS VPLGAAQWGE LKTSAKEPSA GAGEVLLSIS YLPAANRLLV VLIKAKNLHS NQSKELLGKD VSVKVTLKHQ ARKLKKKQTK RAKHKINPVW NEMIMFELPD DLLQASSVEL EVLGQDDSGQ SCALGHCSLG LHTSGSERSH WEEMLKNPRR QIAMWHQLHL
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 :
SDF2 Human, sf9Description:
Stromal Cell-Derived Factor 2, Sf9 Human Recombinant
Stromal Cell Derived Factor 2, Stromal Cell-Derived Factor 2, SDF-2
Product # :
CHM-034Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SDF2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 202 amino acids (19-211a.a.) and having a molecular mass of 22.3kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). SDF2 is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SDF2 protein solution (0.25mg/ml) contains 50mM Tris-HCl (pH 8.0), 10% glycerol, 0.1M NaCl 0.1mM PMSF and 0.5mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Stromal Cell-Derived Factor 2 (SDF2) is a secretory protein which is partly similar to the hydrophilic segments of yeast mannosyltransferases. SDF2 protein’s expression is ubiquitous and the gene is rather conserved among mammals. SDF2 is a protein-coding gene whose alternative splicing results in coding and non-coding variants.
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Synonyms
Stromal Cell Derived Factor 2, Stromal Cell-Derived Factor 2, SDF-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
ADPSSLGVVT CGSVVKLLNT RHNVRLHSHD VRYGSGSGQQ SVTGVTSVDD SNSYWRIRGK SATVCERGTP IKCGQPIRLT HVNTGRNLHS HHFTSPLSGN QEVSAFGEEG EGDYLDDWTV LCNGPYWVRD GEVRFKHSST EVLLSVTGEQ YGRPISGQKE VHGMAQPSQN NYWKAMEGIF MKPSELLKAE AHHAELHHHH HH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TRIAP1 HumanDescription:
TP53 Regulated Inhibitor Of Apoptosis 1 Human Recombinant
TP53 Regulated Inhibitor of Apoptosis 1, P53-Inducible Cell-Survival Factor, Mitochondrial Distribution And Morphology 35 Homolog, Protein 15E1.1, MDM35, WF-1, p53CSV, HSPC132.
Product # :
PRO-1771Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TRIAP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 99 amino acids (1-76 a.a) and having a molecular mass of 11.2kDa.TRIAP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TRIAP1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
TRIAP1 has a p53-binding site in its second exon. TRIAP1 expression is reduced by small interfering RNA enhanced apoptosis, while overexpression of TRIAP1 protects cells from apoptosis triggered by DNA damage. TRIAP1 is highly induced when cells have low levels of genotoxic stresses, but not when DNA damage is severe. TRIAP1 is able to control apoptotic pathways by interacting with Hsp70 which inhibits activity of apoptosis protease activating factor-1.
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Synonyms
TP53 Regulated Inhibitor of Apoptosis 1, P53-Inducible Cell-Survival Factor, Mitochondrial Distribution And Morphology 35 Homolog, Protein 15E1.1, MDM35, WF-1, p53CSV, HSPC132.
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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 MGSMNSVGEA CTDMKREYDQ CFNRWFAEKF LKGDSSGDPC TDLFKRYQQC VQKAIKEKEI PIEGLEFMGH GKEKPENSS
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 :
IFN b AntibodyDescription:
Interferon-beta, Mouse Anti-Human
Leukocyte interferon, B cell interferon, Type I interferon, IFNB1, IFB, IFF, IFNB, IFN-b 1a MGC96956.
Product # :
ANT-185Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Formulation
1mg/ml in PBS (after reconstitution).
More Info
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Introduction
Interferon-beta has antiviral, antibacterial and anticancer activities.
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Synonyms
Leukocyte interferon, B cell interferon, Type I interferon, IFNB1, IFB, IFF, IFNB, IFN-b 1a MGC96956.
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Solubility
Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
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Immunogen
r.Human IFN-b.
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Ig Subclass
Mouse IgG.
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Clone
NYRhIFN-b.
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Titer
By direct ELISA, 1:10,000 dilution will yield 0.5 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
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Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.
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Purification Method
Protein-A.
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 :
Adiponectin Human, HEKDescription:
Adiponectin Human Recombinant, HEK
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-434Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Acrp30 Human Recombinant produced in HEK cells is a glycosylated polypeptide chain containing 234 amino acids (19-244a.a.) and having a molecular mass of 25.5kDa. Acrp30 is expressed with a FLAG tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
HEK293 (Human Embryonic Kidney cell line).
Formulation
Filtered (0.4µm) and lyophilized from 0.5mg/ml in 50mM phosphate Buffer, 75mM NaCl, pH 7.4.
Purity
Greater than 98% as determined by HPLC and SDS PAGE.
Biological Activity
In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.
sds-page
More Info
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Introduction
Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
For long term, store lyophilized AdipoQ 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. The lyophilized protein remains stable for 24 months when stored at -20°C.
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Solubility
Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product not sterile! Please filter the product by an appropriate sterile filter before using it in cell culture.
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Amino Acid Sequence
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.
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Background
What is the molecular weight/Mw of adiponectin Protein?
Adiponectin Protein has a total Mw of 25.5kDa.
What is the source or expression system of adiponectin Protein?
HEK293.
What is the Purity of adiponectin Protein?
adiponectin Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of adiponectin Protein?
In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.
What is the amino acid sequence of adiponectin Protein?
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.
What applications can adiponectin Protein be used in?
adiponectin Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for adiponectin Protein?
The endotoxin level is minimal, adiponectin 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 :
KIAA0101 HumanDescription:
KIAA0101 Human Recombinant
KIAA0101, L5, NS5ATP9, OEATC, OEATC-1, OEATC1, p15(PAF), p15/PAF, p15PAF, PAF, PAF15, PCNA-associated factor, Hepatitis C virus NS5A-transactivated protein 9, HCV NS5A-transactivated protein 9, Overexpressed in anaplastic thyroid carcinoma 1, PCNA-associated factor of 15 kDa.
Product # :
PRO-1683Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KIAA0101 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 134 amino acids (1-111) and having a molecular mass of 14.4 kDa.KIAA0101 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The KIAA0101 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
KIAA0101 is a PCNA-binding protein which performs as a regulator of DNA repair all through DNA replication. Subsequent to DNA mutilation, the collaboration with PCNA is interrupted, enabling the interaction between monoubiquitinated PCNA and the translesion DNA synthesis DNA polymerase eta (POLH) at stalled replisomes, assisting the bypass of replication-fork-blocking lesions. Additionally, KIAA0101 performs as a controller of centrosome number.
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Synonyms
KIAA0101, L5, NS5ATP9, OEATC, OEATC-1, OEATC1, p15(PAF), p15/PAF, p15PAF, PAF, PAF15, PCNA-associated factor, Hepatitis C virus NS5A-transactivated protein 9, HCV NS5A-transactivated protein 9, Overexpressed in anaplastic thyroid carcinoma 1, PCNA-associated factor of 15 kDa.
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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 MGSMVRTKAD SVPGTYRKVV AARAPRKVLG SSTSATNSTS VSSRKAENKY AGGNPVCVRP TPKWQKGIGE FFRLSPKDSE KENQIPEEAG SSGLGKAKRK ACPLQPDHTN DEKE.
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 :
CD90 HumanDescription:
Thy-1 Cell Surface Antigen Human Recombinant
Thy-1 Cell Surface Antigen, Thy-1 Antigen, CDw90, Thy-1 Membrane Glycoprotein, Thy-1 T-Cell Antigen, CD90 Antigen, CD90, THY1.
Product # :
PRO-2346Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CD90 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 117 amino acids (20-130a.a.) and having a molecular mass of 13.3kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-28kDa).CD90 is fused with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CD90 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Thy-1 membrane glycoprotein (CD90) is a cell membrane protein which contains one lg-like V-type (immunoglobulin-like) domain. CD90 protein belongs to the immunoglobulin superfamily of adhesion molecules with constitutive expression on fibroblast cells. CD90 protein is involved in cell adhesion and cell communication in numerous cell types, predominantly in cells of the immune and nervous systems. CD90 may also have a role in cell-cell or cell-ligand interactions during synaptogenesis and other events in the brain. CD90 can be used as a marker for various stem cells and for the axonal processes of mature neurons. CD90 may serve as a tumor suppressor in nasopharyngeal carcinoma.
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Synonyms
Thy-1 Cell Surface Antigen, Thy-1 Antigen, CDw90, Thy-1 Membrane Glycoprotein, Thy-1 T-Cell Antigen, CD90 Antigen, CD90, THY1.
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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
QKVTSLTACL VDQSLRLDCR HENTSSSPIQ YEFSLTRETK KHVLFGTVGV PEHTYRSRTN FTSKYNMKVL YLSAFTSKDE GTYTCALHHS GHSPPISSQN VTVLRDKLVK CHHHHHH.
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 :
TNF a MouseDescription:
Tumor Necrosis Factor-Alpha Mouse Recombinant
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Product # :
CYT-252Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Tumor Necrosis Factor-a Mouse Recombinant produced in E. coli is a single, non glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17301.32 Dalton. The TNF-alpha is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(c) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.1ng/ml, corresponding to a Specific Activity of 10,000,000 Units/mg.More Info
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Introduction
Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer. -
Synonyms
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Tumor Necrosis Factor-alpha in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MLRSSSQNSS DKPVAHVVAN HQVEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLVY SQVLFKGQGC PDYVLLTHTV SRFAISYQEK VNLLSAVKSP CPKDTPEGAE LKPWYEPIYL GGVFQLEKGD QLSAEVNLPK YLDFAESGQV YFGVIAL
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Background
Tumor Necrosis Factor-alpha (TNF-α) is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. It is primarily produced by activated macrophages, but can also be secreted by other immune cells, such as T cells, natural killer cells, and mast cells. TNF-α is involved in a wide range of physiological and pathological processes, including the defense against infections, the development of autoimmune diseases, and the progression of cancer.
TNF-α exerts its effects by binding to two distinct cell surface receptors, TNF receptor 1 (TNFR1) and TNF receptor 2 (TNFR2). Upon binding to its receptors, TNF-α activates multiple signaling pathways, including the nuclear factor-kappa B (NF-κB) pathway, the mitogen-activated protein kinase (MAPK) pathway, and the apoptotic pathway. These signaling pathways regulate various cellular processes, such as inflammation, cell proliferation, differentiation, and apoptosis.
In the context of infections, TNF-α plays a crucial role in the body's defense against pathogens. It promotes the recruitment and activation of immune cells, enhances the production of other pro-inflammatory cytokines, and stimulates the expression of adhesion molecules on endothelial cells, facilitating the migration of immune cells to the site of infection. TNF-α also helps to induce fever, which is an important component of the body's immune response to infections.
However, excessive or prolonged production of TNF-α can contribute to the development of chronic inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and psoriasis. In these conditions, elevated levels of TNF-α promote the infiltration of immune cells into the affected tissues, leading to tissue damage and the perpetuation of inflammation. The central role of TNF-α in the pathogenesis of these diseases has led to the development of anti-TNF-α therapies, which have revolutionized the treatment of chronic inflammatory diseases. These therapies include monoclonal antibodies, such as infliximab and adalimumab, and soluble TNF receptor fusion proteins, such as etanercept. Anti-TNF-α therapies have been shown to be effective in reducing inflammation, improving symptoms, and slowing disease progression in patients with chronic inflammatory diseases.
In the context of cancer, TNF-α has complex and context-dependent effects on tumor development and progression. On one hand, TNF-α can promote anti-tumor immunity by activating immune cells and stimulating the production of other pro-inflammatory cytokines. On the other hand, chronic inflammation driven by TNF-α can promote tumor growth, angiogenesis, and metastasis. Therefore, the role of TNF-α in cancer is still an area of active research, and the development of TNF-α-targeted therapies for cancer remains a challenge.
In conclusion, TNF-α is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. Its involvement in various physiological and pathological processes has made it an important target for the development of therapies for chronic inflammatory diseases and cancer. Anti-TNF-α therapies have revolutionized the treatment of chronic inflammatory diseases, but the complex role of TNF-α in cancer remains an area of ongoing research. Understanding the precise mechanisms by which TNF-α contributes to disease pathogenesis will be crucial for the development of more effective and targeted therapies.
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Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.24 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 calibrated solution of TNF-a 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.
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Name :
SPARC HumanDescription:
Secreted Protein Acidic & Rich in Cysteine Recombinant Human
Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine.
Product # :
PRO-2602Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Secreted Protein Acidic & Rich in Cysteine Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 286 amino acids and having a molecular mass of 32.7kDa.SPARC is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by its ability to inhibit the cell growth of Mv1Lu mink lung epithelial cells is < 3.0 µg/mL, corresponding to a specific activity of > 333 IU/mg.
More Info
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Introduction
SPARC, an acronym for “secreted protein, acidic and rich in cysteine”, is also known as osteonectin or BM-40. It is the founding member of a family of secreted matricellular proteins with similar domain structure. The 303 amino acid, 43 kDa protein contains a 17 aa signal sequence, an N-terminal acidic region that binds calcium, a follistatin domain containing Kazal-like sequences, and a C-terminal extracellular calcium (EC) binding domain with two EF-hand motifs. SPARC is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, especially in areas of tissue morphogenesis and remodeling. SPARC shows context-specific effects, but generally inhibits adhesion, spreading and proliferation, and promotes collagen matrix formation. For endothelial cells, SPARC disrupts focal adhesions and binds and sequesters PDGF and VEGF. SPARC is abundantly expressed in bone, where it promotes osteoblast differentiation and inhibits adipogenesis.
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Synonyms
Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SPARC although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Secreted Protein Acidic & Rich in Cysteine 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 SPARC 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
APQQEALPDE TEVVEETVAE VTEVSVGANP VQVEVGEFDD GAEETEEEVV AENPCQNHHC KHGKVCELDE NNTPMCVCQD PTSCPAPIGE FEKVCSNDNK TFDSSCHFFA TKCTLEGTKK GHKLHLDYIG PCKYIPPCLD SELTEFPLRM RDWLKNVLVT LYERDEDNNL LTEKQKLRVK KIHENEKRLE AGDHPVELLA RDFEKNYNMY IFPVHWQFGQ LDQHPIDGYL SHTELAPLRA PLIPMEHCTT RFFETCDLDN DKYIALDEWA GCFGIKQKDI DKDLVI.
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 :
Epoetin Fc HumanDescription:
Erythropoietin-Alpha Fc-Chimera Human Recombinant
EPO-a, EPO-alpha, Epoetin, EP, MGC138142.
Product # :
CYT-325Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Erythropoietin-alpha Fc-Chimera Human Recombinant is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a dimeric, glycosilated, polypeptide chain consisting of two mature human EPO molecules linked to the Fc portion of human IgG1. The Fc component contains the CH2 domain, the CH3 domain and hinge region, but not the CH1 domain of IgG1. As a result of glycosylation, the recombinant protein migrates with an apparent molecular mass of 140 kDa in non-reducing SDS-PAGE.
Source
Chinese Hamster Ovary Cells(CHO).
Formulation
Each mg of lyophilized powder contains 1x 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 as determined by the dose-dependent stimulation of human megakaryoblastic leukemia cells is less than 2.0 ng/ml, corresponding to a Specific Activity of 5.0 x 105 IU/mg.More Info
-
Introduction
This gene is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.
-
Synonyms
EPO-a, EPO-alpha, Epoetin, EP, MGC138142.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Erythropoietin-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EPO-alpha 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 Erythropoietin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Background
What is the molecular weight/Mw of EPOETIN Protein?
EPOETIN Protein has a total Mw of 140kDa.
What is the source or expression system of EPOETIN Protein?
Chinese Hamster Ovary Cells(CHO).
What is the Purity of EPOETIN Protein?
EPOETIN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EPOETIN Protein?
The ED50 as determined by the dose-dependent stimulation of human megakaryoblastic leukemia cells is less than 2.0 ng/ml, corresponding to a Specific Activity of 5.0 x 105 IU/mg.
What applications can EPOETIN Protein be used in?
EPOETIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EPOETIN Protein?
The endotoxin level is minimal, EPOETIN 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 :
SIGLEC5 HumanDescription:
Sialic Acid Binding Ig Like Lectin 5 Human Recombinant
Sialic Acid Binding Ig Like Lectin 5, Obesity-Binding Protein 2, OB-Binding Protein 2, CD33 Antigen-Like 2, SIGLEC-5, CD33L2, OB-BP2, OBBP2, Sialic Acid-Binding Immunoglobulin-Like Lectin 5, Sialic Acid Binding Ig-Like Lectin 5, Sialic Acid-Binding Ig-Like Lectin 5, CD170 Antigen, CD170, Sialic acid-binding Ig-like lectin 5, Siglec-5, CD33 antigen-like 2, Obesity-binding protein 2, OB-BP2, OB-binding protein 2, CD170.
Product # :
PRO-2432Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
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- More Info
Description
SIGLEC5 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 667 amino acids (17-441a.a.) and having a molecular mass of 74.2kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). SIGLEC5 is expressed with a 239 amino acid hIgG-His Tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SIGLEC5 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Sialic Acid Binding Ig Like Lectin 5, also known as SIGLEC5 is a member of the immunoglobulin superfamily and SIGLEC family. SIGLEC5 contains of 2 Ig-like C2-type domains and 1 Ig-like V-type domain. In addition, SIGLEC5 is expressed by monocytic/myeloid lineage cells. SIGLEC5 is expressed at high levels in peripheral blood leukocytes, spleen, and at lower levels in lymph node, appendix, pancreas, lung, and thymus.
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Synonyms
Sialic Acid Binding Ig Like Lectin 5, Obesity-Binding Protein 2, OB-Binding Protein 2, CD33 Antigen-Like 2, SIGLEC-5, CD33L2, OB-BP2, OBBP2, Sialic Acid-Binding Immunoglobulin-Like Lectin 5, Sialic Acid Binding Ig-Like Lectin 5, Sialic Acid-Binding Ig-Like Lectin 5, CD170 Antigen, CD170, Sialic acid-binding Ig-like lectin 5, Siglec-5, CD33 antigen-like 2, Obesity-binding protein 2, OB-BP2, OB-binding protein 2, CD170.
-
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
ADLEKPVYEL QVQKSVTVQE GLCVLVPCSF SYPWRSWYSS PPLYVYWFRD GEIPYYAEVV ATNNPDRRVK PETQGRFRLL GDVQKKNCSL SIGDARMEDT GSYFFRVERG RDVKYSYQQN KLNLEVTALI EKPDIHFLEP LESGRPTRLS CSLPGSCEAG PPLTFSWTGN ALSPLDPETT RSSELTLTPR PEDHGTNLTC QMKRQGAQVT TERTVQLNVS YAPQTITIFR NGIALEILQN TSYLPVLEGQ ALRLLCDAPS NPPAHLSWFQ GSPALNATPI SNTGILELRR VRSAEEGGFT CRAQHPLGFL QIFLNLSVYS LPQLLGPSCS WEAEGLHCRC SFRARPAPSL CWRLEEKPLE GNSSQGSFKV NSSSAGPWAN SSLILHGGLS SDLKVSCKAW NIYGSQSGSV LLLQGRSNLG TGVVPAALLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.
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 :
MMP9 Human, HEKDescription:
Matrix Metalloproteinase-9 Human Recombinant, HEK
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.
Product # :
ENZ-1084Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
MMP9 Human Recombinant is a single, glycosylated polypeptide chain containing 694 amino acids (20-707a.a) and having a molecular mass of 77.2kDa (calculated). MMP9 is fused to a 6 a.a His tag at C-terminal.
Source
HEK293 Cells.
Formulation
MMP9 filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in PBS, pH7.5 and 5% (w/v) Threalose.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Matrix metalloproteinases are a family of zinc and calcium-dependent endopeptidases that break down extracellular matrix proteins. The MMP9 is secreted as a 92kDa zymogen. Cleavage of ProMMP-9 results in the active enzyme, having a molecular weight of approximately 82kDa. MMP9 is composed of the following domains: a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. MMP9 is produced by the several cell types: monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts and endothelial cells. MMP9 is involved in inflammatory responses, tissue remodeling, wound healing, tumor growth and metastasis. MMP9 may also play an important part in local proteolysis of the extracellular matrix and in leukocyte migration, as well as in bone osteoclastic resorption. MMP9 cleaves type IV and type V collagens into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. MMP9 can also degrade fibronectin but not laminin or Pz-peptide.
MMP9 defects may be a cause of susceptibility to intervertebral disc disease (IDD), also known as lumbar disk herniation (LDH). -
Synonyms
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
APRQRQSTLVLFPGDLRTNLTDRQLAEEYLYRYGYTRVAEMRGESKSLGPALLLLQKQLSLPET
GELDSATLKAMRTPRCGVPDLGRFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAF
ALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDD
ELWSLGKGVVVPTRFGNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFG
FCPSERLYTRDGNADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFCPTR
ADSTVMGGNSAGELCVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFCPDQ
GYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPPLHKDDVNGIRHLYGPRPEPEPRPPTTTT
PQPTAPPTVCPTGPPTVHPSERPTAGPTGPPSAGPTGPPTAGPSTATTVPLSPVDDACNVNIFDAIAE
IGNQLYLFKDGKYWRFSEGRGSRPQGPFLIADKWPALPRKLDSVFEERLSKKLFFFSGRQVWVYTGAS
VLGPRRLDKLGLGADVAQVTGALRSGRGKMLLFSGRRLWRFDVKAQMVDPRSASEVDRMFPGVPLD
THDVFQYREKAYFCQDRFYWRVSSRSELNQVDQVGYVTYDILQCPEDHHHHHH.
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 :
BLNK HumanDescription:
B-Cell Linker Human Recombinant
B-cell linker protein, B-cell adapter containing a SH2 domain protein, B-cell adapter containing a Src homology 2 domain protein, Cytoplasmic adapter protein, Src homology 2 domain-containing leukocyte protein of 65 kDa, SLP-65, BLNK, BASH, SLP65, AGM4, LY57, BLNK-S, MGC111051.
Product # :
PRO-102Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- formulation
- purity
- More Info
Description
BLNK Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 476 amino acids (1-456 a.a.) and having a molecular mass of 52.6kDa (Molecular weight on SDS-PAGE will appear higher). The BLNK is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BLNK solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl, 1mM DTT and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
BLNK is a cytoplasmic linker or adaptor protein which has a significant role in B cell development. B-cell linker (BLNK) is essential for normal B-cell development. BLNK bridges B cell receptor-associated kinase activation with downstream signaling pathways, thus affecting different biological functions. BLNK associates with the effector proteins GRB2, Vav, NCK and PLC-g following activation of the B cell receptor. BLNK is phosphorylated by the Syk tyrosine kinase, which in turn permits activation of downstream effector proteins including GRB2 and PLC-g. Mutations in the BLNK gene cause hypoglobulinemia and absent B cells, a disease in which the pro- to pre-B-cell transition is developmentally blocked. Deficiency in the BLNK protein is seen in some cases of pre-B acute lymphoblastic leukemia.
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Synonyms
B-cell linker protein, B-cell adapter containing a SH2 domain protein, B-cell adapter containing a Src homology 2 domain protein, Cytoplasmic adapter protein, Src homology 2 domain-containing leukocyte protein of 65 kDa, SLP-65, BLNK, BASH, SLP65, AGM4, LY57, BLNK-S, MGC111051.
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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 MDKLNKITVP ASQKLRQLQK MVHDIKNNEG GIMNKIKKLK VKAPPSVPRR DYASESPADE EQQWSDDFDS DYENPDEHSD SEMYVMPAEE NADDSYEPPP VEQETRPVHP ALPFARGEYI DNRSSQRHSP PFSKTLPSKP SWPSEKARLT STLPALTALQ KPQVPPKPKG LLEDEADYVV PVEDNDENYI HPTESSSPPP EKAPMVNRST KPNSSTPASP PGTASGRNSG AWETKSPPPA APSPLPRAGK KPTTPLKTTP VASQQNASSV CEEKPIPAER HRGSSHRQEA VQSPVFPPAQ KQIHQKPIPL PRFTEGGNPT VDGPLPSFSS NSTISEQEAG VLCKPWYAGA CDRKSAEEAL HRSNKDGSFL IRKSSGHDSK QPYTLVVFFN KRVYNIPVRF IEATKQYALG RKKNGEEYFG SVAEIIRNHQ HSPLVLIDSQ NNTKDSTRLK YAVKVS.
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 :
CD105 Human, HisDescription:
Endoglin Human Recombinant, His-Tag
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
Product # :
CYT-823Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- sds-page
Description
Endoglin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 594 amino acids (26-586) and having a molecular mass of 64.9 kDa. Endoglin is fused to a 36 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The Endoglin solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 150mM NaCl and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
sds-page
More Info
-
Introduction
Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.The Endoglin protein consists of a homodimer of 180 kDA with disulfide links. Endoglin has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Furthermore, Endoglin has been found to be part of the TGF-beta1 receptor complex. Endoglin thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Endoglin expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities.
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Synonyms
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSETVH CDLQPVGPER DEVTYTTSQV SKGCVAQAPN AILEVHVLFL EFPTGPSQLE LTLQASKQNG TWPREVLLVL SVNSSVFLHL QALGIPLHLA YNSSLVTFQE PPGVNTTELP SFPKTQILEW AAERGPITSA AELNDPQSIL LRLGQAQGSL SFCMLEASQD MGRTLEWRPR TPALVRGCHL EGVAGHKEAH ILRVLPGHSA GPRTVTVKVE LSCAPGDLDA VLILQGPPYV SWLIDANHNM QIWTTGEYSF KIFPEKNIRG FKLPDTPQGL LGEARMLNAS IVASFVELPL ASIVSLHASS CGGRLQTSPA PIQTTPPKDT CSPELLMSLI QTKCADDAMT LVLKKELVAH LKCTITGLTF WDPSCEAEDR GDKFVLRSAY SSCGMQVSAS MISNEAVVNI LSSSSPQRKK VHCLNMDSLS FQLGLYLSPH FLQASNTIEP GQQSFVQVRV SPSVSEFLLQ LDSCHLDLGP EGGTVELIQG RAAKGNCVSL LSPSPEGDPR FSFLLHFYTV PIPKTGTLSC TVALRPKTGS QDQEVHRTVF MRLNIISPDL SGCTSKG
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Background
What is the molecular weight/Mw of CD105 Protein?
CD105 Protein has a total Mw of 64.9kDa.
What is the source or expression system of CD105 Protein?
Escherichia Coli.
What is the Purity of CD105 Protein?
CD105 Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of CD105 Protein?
The biological functionality of CD105 Protein will be determined in the future.
What is the amino acid sequence of CD105 Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSETVH CDLQPVGPER DEVTYTTSQV SKGCVAQAPN AILEVHVLFL EFPTGPSQLE LTLQASKQNG TWPREVLLVL SVNSSVFLHL QALGIPLHLA YNSSLVTFQE PPGVNTTELP SFPKTQILEW AAERGPITSA AELNDPQSIL LRLGQAQGSL SFCMLEASQD MGRTLEWRPR TPALVRGCHL EGVAGHKEAH ILRVLPGHSA GPRTVTVKVE LSCAPGDLDA VLILQGPPYV SWLIDANHNM QIWTTGEYSF KIFPEKNIRG FKLPDTPQGL LGEARMLNAS IVASFVELPL ASIVSLHASS CGGRLQTSPA PIQTTPPKDT CSPELLMSLI QTKCADDAMT LVLKKELVAH LKCTITGLTF WDPSCEAEDR GDKFVLRSAY SSCGMQVSAS MISNEAVVNI LSSSSPQRKK VHCLNMDSLS FQLGLYLSPH FLQASNTIEP GQQSFVQVRV SPSVSEFLLQ LDSCHLDLGP EGGTVELIQG RAAKGNCVSL LSPSPEGDPR FSFLLHFYTV PIPKTGTLSC TVALRPKTGS QDQEVHRTVF MRLNIISPDL SGCTSKG
What applications can CD105 Protein be used in?
CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CD105 Protein?
The endotoxin level is minimal, CD105 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 :
CNTFR Human, Sf9Description:
Ciliary Neurotrophic Factor Receptor Human Recombinant, Sf9
Ciliary Neurotrophic Factor Receptor, CNTF Receptor Subunit Alpha, CNTFR-Alpha, Ciliary Neurotrophic Factor Receptor Subunit Alpha.
Product # :
CYT-1087Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
- More Info
Description
CTNFR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 329 amino acids (23-342a.a.) and having a molecular mass of 36.9kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).CTNFR is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CTNFR protein solution (1mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Ciliary Neurotrophic Factor Receptor (CNTFR) is a member of the type I cytokine receptor family and binds to CNTF. The alpha subunit provides the receptor specificity. Sole nucleotide polymorphisms in CNTFR has been associated with variations in muscle strength, in addition to early onset of eating disorders.
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Synonyms
Ciliary Neurotrophic Factor Receptor, CNTF Receptor Subunit Alpha, CNTFR-Alpha, Ciliary Neurotrophic Factor Receptor Subunit Alpha.
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Physical Appearance
Sterile Filtered colorless 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
ADPQRHSPQE APHVQYERLG SDVTLPCGTA NWDAAVTWRV NGTDLAPDLL NGSQLVLHGL ELGHSGLYAC FHRDSWHLRH QVLLHVGLPPREPVLSCRSN TYPKGFYCSW HLPTPTYIPN TFNVTVLHGS KIMVCEKDPA LKNRCHIRYM HLFSTIKYKV SISVSNALGH NATAITFDEF TIVKPDPPEN VVARPVPSNP RRLEVTWQTP STWPDPESFP LKFFLRYRPL ILDQWQHVEL SDGTAHTITD AYAGKEYIIQ VAAKDNEIGTWSDWSVAAHA TPWTEEPRHL TTEAQAAETT TSTTSSLAPP PTTKICDPGE LGSHHHHHH.
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Background
What is the molecular weight/Mw of CNTFR Protein?
CNTFR Protein has a total Mw of 36.9kDa.
What is the source or expression system of CNTFR Protein?
Sf9, Baculovirus cells.
What is the Purity of CNTFR Protein?
CNTFR Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CNTFR Protein?
The biological functionality of CNTFR Protein will be determined in the future.
What is the amino acid sequence of CNTFR Protein?
ADPQRHSPQE APHVQYERLG SDVTLPCGTA NWDAAVTWRV NGTDLAPDLL NGSQLVLHGL ELGHSGLYAC FHRDSWHLRH QVLLHVGLPPREPVLSCRSN TYPKGFYCSW HLPTPTYIPN TFNVTVLHGS KIMVCEKDPA LKNRCHIRYM HLFSTIKYKV SISVSNALGH NATAITFDEF TIVKPDPPEN VVARPVPSNP RRLEVTWQTP STWPDPESFP LKFFLRYRPL ILDQWQHVEL SDGTAHTITD AYAGKEYIIQ VAAKDNEIGTWSDWSVAAHA TPWTEEPRHL TTEAQAAETT TSTTSSLAPP PTTKICDPGE LGSHHHHHH.
What applications can CNTFR Protein be used in?
CNTFR Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CNTFR Protein?
The endotoxin level is minimal, CNTFR 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 :
HK1 AntibodyDescription:
Hexokinase-1, Mouse Anti Human
Hexokinase-1, EC 2.7.1.1, Hexokinase type I, HK I, Brain form hexokinase, HK1-ta, HK1-tb, HXK1, HK1.
Product # :
ANT-375Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
More Info
-
Introduction
Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. Hexokinase1 encodes a ubiquitous form of hexokinase which localizes to the outer membrane of mitochondria. Mutations in this gene have been associated with hemolytic anemia due to hexokinase deficiency. Alternative splicing of HXK1 results in five transcript variants which encode different isoforms, some of which are tissue-specific. Each isoform has a distinct N-terminus; the remainder of the protein is identical among all the isoforms. A sixth transcript variant has been described, but due to the presence of several stop codons, it is not thought to encode a protein.
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Synonyms
Hexokinase-1, EC 2.7.1.1, Hexokinase type I, HK I, Brain form hexokinase, HK1-ta, HK1-tb, HXK1, HK1.
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Physical Appearance
Sterile Filtered clear solution.
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Immunogen
Anti-human Hexokinase-1 mAb is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human Hexokinase-1 amino acids 1-917 purified from E. coli.
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Ig Subclass
Mouse IgG2a heavy chain and κ light chain.
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Clone
P4D7AT.
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Applications
Hexokinase-1 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. Recommended dilution range for Western blot analysis is 1:1,000 ~ 2,000. Recommended starting dilution is 1:1,000.
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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
Hexokinase-1 antibody was purified from mouse ascitic fluids by protein-G 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.
- View Data Sheet
Name :
MIP 1a Mouse, HisDescription:
Macrophage Inflammatory Protein-1 Alpha Mouse Recombinant (CCL3), His Tag
Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA, TY-5, SIS-alpha, Heparin-binding chemotaxis protein, L2G25B.
Product # :
CHM-008Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
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Description
MIP-1a Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids (24-92 a.a.) and having a molecular mass of 10.4kDa.MIP-1a is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MIP-1a protein solution (0.5mg/ml) containing 20mM Sodium citrate buffer (pH 3.5) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-a from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.
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Synonyms
Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA, TY-5, SIS-alpha, Heparin-binding chemotaxis protein, L2G25B.
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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 MGSMAPYGAD TPTACCFSYS RKIPRQFIVD YFETSSLCSQ PGVIFLTKRN RQICADSKET WVQEYITDLE LNA.
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Background
What is the molecular weight/Mw of MIP 1A MOUSE, HIS Protein?
MIP 1A MOUSE, HIS Protein has a total Mw of 10.4kDa.
What is the source or expression system of MIP 1A MOUSE, HIS Protein?
Escherichia Coli.
What is the Purity of MIP 1A MOUSE, HIS Protein?
MIP 1A MOUSE, HIS Protein is > 90% pure as determined by SDS-PAGE.
What is the Biological Activity of MIP 1A MOUSE, HIS Protein?
The biological functionality of MIP 1A MOUSE, HIS Protein will be determined in the future.
What is the amino acid sequence of MIP 1A MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSMAPYGAD TPTACCFSYS RKIPRQFIVD YFETSSLCSQ PGVIFLTKRN RQICADSKET WVQEYITDLE LNA..
What applications can MIP 1A MOUSE, HIS Protein be used in?
MIP 1A MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for MIP 1A MOUSE, HIS Protein?
The endotoxin level is minimal, MIP 1A MOUSE, 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 :
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
- source
- formulation
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- SDS-PAGE
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
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.
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 :
Tetanus antibodyDescription:
Tetanus toxoid scFv Recombinant antibody
Product # :
ANT-195Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- purity
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Description
Tetanus toxin is the neurotoxin produced by the vegetative spore of Clostridium tetani in anaerobic conditions, causing tetanus.Recombinant Anti Tetanus produced in E.Coli is a non-glycosylated, polypeptide chain containing a hexahistidine tag and having a molecular weight of 37 kDa.Tetanus Antibody is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Tetanus is supplied in 1x PBS (pH 7.4) and 0.09% azide
Purity
Greater than 95.0% as determined byAnalysis by RP-HPLC.
Analysis by SDS-PAGE.More Info
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
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Type
Antibody Recombinant.
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 :
KHDC1L HumanDescription:
KH Homology Domain Containing 1-Like Human Recombinant
KH Homology Domain Containing 1-Like, RP11-257K9.7, Putative KHDC1-Like Protein.
Product # :
PRO-1720Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KHDC1L Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 151 amino acids (1-128 a.a) and having a molecular mass of 16.9kDa.KHDC1L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
KHDC1L protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
KH homology domain containing 1-like, also known as KHDC1L is a member of the KHDC1 family.KHDC1L is a protein-coding gene; an important paralog of this gene is KHDC1.
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Synonyms
KH Homology Domain Containing 1-Like, RP11-257K9.7, Putative KHDC1-Like Protein.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. 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 MGSMAVGTSA LSKEPWWTLP ENFHSPMVFH MEEDQEELIF GLDDTYLRCI ELHSHTLIQL ERCFTATGQT RVTVVGPPMA KQWLLLMFHC VGSQDSKCHA RGLKMLERVR SQPLTNDDLV TSVSLPPYTG D.
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 :
Procalcitonin MouseDescription:
Procalcitonin Mouse Recombinant
Calcitonin, Calca, Calc.
Product # :
HOR-014Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Procalcitonin Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Val26-Ser136) containing 121 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 13.6kDa.
Source
Escherichia Coli.
Formulation
Procalcitonin was filtered (0.4 µm) and lyophilized in 20mM Tris buffer and 50mM NaCl, pH 7.5.
Purity
Greater than 94.0% as determined by SDS-PAGE.
More Info
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Introduction
Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.
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Synonyms
Calcitonin, Calca, Calc.
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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. Procalcitonin 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
MKHHHHHHASVPLRSILESS PGMATLSEEE VRLLAALVQD YMQMKARELE QEEEQEAEGS SLDSPRSKRC GNLSTCMLGT YTQDLNKFHT FPQTSIGVEA PGKKRDVAKD LETNHQSHFG N.
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 :
LGALS2 Mouse, ActiveDescription:
Galectin-2, BioActive Mouse Recombinant
Galectin-2, Gal-2, Lgals2, 2200008F12Rik, AI324147.
Product # :
CYT-1155Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
LGALS2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids (1-130 a.a) and having a molecular mass of 17.3kDa.LGALS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
LGALS2 protein (1mg/ml) contains 10% glycerol, 0.1M NaCl, 1mM DTT and 20mM Tris-HCl buffer (pH 8.0).
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Measured by its ability to agglutinate human red blood cells. The ED50 is ≥ 20ug/ml.
More Info
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Introduction
Galectin-2 or LGALS2 is a protein, part of the galectin proteins family. The galectin proteins family holds galectin proteins family lectins that mediates adhesion between cells or cells to ECM. This family also take part in pre-mRNA splicing, apoptosis & tumor progression. Galectin-2 induces apoptosis in T cells that are activated & binds to lymphotoxin-a, also can implicatate on myocardial infarction. LGALS2 from human and mouse share about 65% amino acid sequence resemblance.
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Synonyms
Galectin-2, Gal-2, Lgals2, 2200008F12Rik, AI324147.
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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 MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE
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Background
What is the molecular weight/Mw of LGALS2 MOUSE, ACTIVE Protein?
LGALS2 MOUSE, ACTIVE Protein has a total Mw of 17.3kDa.
What is the source or expression system of LGALS2 MOUSE, ACTIVE Protein?
Escherichia Coli.
What is the Purity of LGALS2 MOUSE, ACTIVE Protein?
LGALS2 MOUSE, ACTIVE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS2 MOUSE, ACTIVE Protein?
Measured by its ability to agglutinate human red blood cells. The ED50 is ≥ 20ug/ml.
What is the amino acid sequence of LGALS2 MOUSE, ACTIVE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE.
What applications can LGALS2 MOUSE, ACTIVE Protein be used in?
LGALS2 MOUSE, ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS2 MOUSE, ACTIVE Protein?
The endotoxin level is minimal, LGALS2 MOUSE, ACTIVE 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 :
CMV Pp28Description:
Cytomegalo Virus Pp28 (UL99) Recombinant
Product # :
CMV-212Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
- formulation
- purity
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Description
The E.Coli derived recombinant protein contains the CMV Pp28 (UL99) immunodominant regions, 130-160 amino acids.
Source
Escherichia Coli.
Formulation
50mM Tris-Hcl pH 7.2, 1mM EDTA and 50% glycerol.
Purity
CMV Pp28 protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
The human cytomegalovirus UL99-encoded pp28 is a myristylated phosphoprotein that is a constituent of the virion. The pp28 protein is positioned within the tegument of the virus particle, a protein structure that resides between the capsid and envelope. In the infected cell, pp28 is found in a cytoplasmic compartment derived from the Golgi apparatus, where the virus buds into vesicles to acquire its final membrane.
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Stability
CMV Pp28 protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
CMV Pp28 antigen is suitable for ELISA and Western blots, excellent antigen for detection of CMV with minimal specificity problems.
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Specificity
Immunoreactive with sera of CMV-infected individuals.
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Purification Method
Purified by GS-4B Sepharose-Affinity Purification.
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 :
NCR3LG1 HumanDescription:
Natural Cytotoxicity Triggering Receptor 3 Ligand 1 Human Recombinant
B7H6, B7-H6, B7 Homolog 6
Product # :
PRO-2762Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- biological activity
- More Info
Description
NCR3LG1 Human Recombinant produced in HEK is a single, glycosylated polypeptide chain containing 477 amino acids (25-262 a.a) and having a molecular mass of 53.6 kDa. NCR3LG1 is fused to a 239 amino acid hIgG-His tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 Cells
Formulation
NCR3LG1 protein solution (0.5mg/ml) containing 1X PBS (pH-7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Measured in a functional ELISA with Human NCR3. The ED50 range ≤500 ng/ml.
More Info
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Introduction
The B7 proteins are crucial in the regulation of the adaptive immune system. Among them is NCR3LG1. NCR3LG1 is part of the B7 family and is expressed on tumor cells. NCR3LG1 Interaction with NKp30 protein results in cytotoxicity and natural killer cell activation.Humans and rats have a single NCR3LG1 gene; though, numerous B7H6 genes were detected in a single large cluster in the Xenopus genome. NCR3LG1, a ligand for the NK cell activating receptor NKp30, targest to produce CAR that targets multiple tumor types. NCR3LG1 is expressed on many primary human tumors, including leukemia, lymphoma and gastrointestinal stromal tumors, though it is not constitutively expressed on normal tissues.
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Synonyms
B7H6, B7-H6, B7 Homolog 6
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
DLKVEMMAGG TQITPLNDNV TIFCNIFYSQ PLNITSMGIT WFWKSLTFDK EVKVFEFFGD HQEAFRPGAI VSPWRLKSGD ASLRLPGIQL EEAGEYRCEV VVTPLKAQGT VQLEVVASPA SRLLLDQVGM KENEDKYMCE SSGFYPEAIN ITWEKQTQKF PHPIEISEDV ITGPTIKNMD GTFNVTSCLK LNSSQEDPGT VYQCVVRHAS LHTPLRSNFT LTAARHSLSE TEKTDNFS
LE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH
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.