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1000 results found for “killer cell”
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Name :
sCD40L MouseDescription:
Soluble CD-40 Ligand/TRAP Mouse Recombinant
CD40-L, Tumor necrosis factor ligand superfamily member 5, TNF-related activation protein, TRAP, T cell antigen Gp39, CD154 antigen, sCD40, IGM, IMD3, HIGM1, T-BAM, TNFSF5, hCD40L.
Product # :
CYT-472Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
sCD40 Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 149 amino acids and having a molecular mass of 16409 Dalton. The sCD40 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a sterile concentrated solution (1mg/ml) with 10mM Sodium Phosphate pH=7.5.
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 induce MIP-1 alpha & TNF-alpha from mouse splenocytes was found to be 0.1µg/ml corresponding to a Specific Activity of 10,000IU/mg.
More Info
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Introduction
CD40L or CD154 is a membrane glycoprotein and differentiation antigen expressed on the surface of T-cells. The CD40 ligand stimulates B-cell proliferation and secretion of all immunoglobulin isotypes in the presence of cytokines . CD40 ligand has been shown to induce cytokine production and tumoricidal activity in peripheral blood monocytes. It also costimulates proliferation of activated T-cells and this is accompanied by the production of IFN-gamma , TNF-alpha , and IL2 .
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Synonyms
CD40-L, Tumor necrosis factor ligand superfamily member 5, TNF-related activation protein, TRAP, T cell antigen Gp39, CD154 antigen, sCD40, IGM, IMD3, HIGM1, T-BAM, TNFSF5, hCD40L.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized sCD40 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CD154 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 sCD40 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
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Gln-Arg-Gly-Asp.
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 :
LIF MouseDescription:
Leukemia Inhibitory Factor Mouse Recombinant
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
Product # :
CYT-645Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leukemia Inhibitory Factor (LIF) Murine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 181 amino acids and having a molecular mass of 20 kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Leukemia Inhibitory Factor (LIF) was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM Phosphate buffer pH-7.4 and 0.02% Tween-20.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Activity of murine LIF was determined by the M1 cell differentiation assay which was found to be < 0.01 ng/ml, corresponding to a specific activity of 100,000,000 IU/mg.
A standard of 50 Units is defined as the concentration of mouse LIF in 1.0 mL of tissue culture medium that induces the differentiation of 50% of M1 colonies.More Info
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Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
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Synonyms
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leukemia Inhibitory Factor (LIF) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leukemia Inhibitory Factor (LIF) 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 Leukemia Inhibitory Factor (LIF) in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MSPLPITPVNATCAIRHPCHGNLMNQIKNQLAQLNGSANALFISYYTAQGEPFP NNVEKLCAPNMTDFPSFHGNGTEKTKLVELYRMVAYLSASLTNITRDQKVLNP TAVSLQVKLNATIDVMRGLLSNVLCRLCNKYRVGHVDVPPVPDHSDKEAFQR KKLGCQLLGTYKQVISVVVQAF.
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 :
CDK5 HumanDescription:
Cyclin-dependent Kinase 5 Human Recombinant
Cyclin-dependent kinase 5, Cell division protein kinase 5, Serine/threonine-protein kinase PSSALRE, Tau protein kinase II catalytic subunit, CDK5, CDKN5, TPKII catalytic subunit, cyclin dependent kinase 5.
Product # :
PKA-047Price :
Quantity :
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Shipped with Ice Packs
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Description
CDK5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-292) and having a molecular mass of 35.8kDa. CDK5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CDK5 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol 0.4M Urea.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Cell division protein kinase 5 (CDK5) belongs to the cyclin-dependent kinase family. CDK5 is essential for appropriate development of the brain and in order to be activated CDK5 must link to CDK5R1 or CDK5R2. CDK5 doesn't need phosphorylation on the T loop so that binding with the activator is enough to activate the kinase. CDK5 is engaged in the processes of neuronal maturation and migration, phosphorylating the central intracellular adaptor of the reeling signaling chain.
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Synonyms
Cyclin-dependent kinase 5, Cell division protein kinase 5, Serine/threonine-protein kinase PSSALRE, Tau protein kinase II catalytic subunit, CDK5, CDKN5, TPKII catalytic subunit, cyclin dependent kinase 5.
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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 MGSHMQKYEK LEKIGEGTYG TVFKAKNRET HEIVALKRVR LDDDDEGVPS SALREICLLK ELKHKNIVRL HDVLHSDKKL TLVFEFCDQD LKKYFDSCNG DLDPEIVKSF LFQLLKGLGF CHSRNVLHRD LKPQNLLINR NGELKLADFG LARAFGIPVR CYSAEVVTLW YRPPDVLFGA KLYSTSIDMW SAGCIFAELA NAGRPLFPGN DVDDQLKRIF RLLGTPTEEQ WPSMTKLPDY KPYPMYPATT SLVNVVPKLN ATGRDLLQNL LKCNPVQRIS AEEALQHPYF SDFCPP.
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 1 beta Human, HisDescription:
Interleukin-1 beta Human Recombinant, His Tag
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
Product # :
CYT-480Price :
Quantity :
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Shipped with Ice Packs
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Description
Interleukin-1 beta His-Tag Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 153 amino acids fragment (117-269) and having a total molecular mass of 21.88 kDa fused with an amino-terminal hexahistidine tag. The IL-1b His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL-1b His tag protein solution is supplied in 20mM Tris-HCl pH 8.0 and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Interleukin-1b is a potent pro-inflammatory cytokine produced by a wide variety of cell types including monocytes and macrophages. It displays a broad range of biological activity including activation of B and T cells in response to inflammation and the activation of endothelial cells.
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Synonyms
Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.
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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.
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Amino Acid Sequence
APVRSLNCTLRDSQQKSLVMSGPYELKALHLQGQDMEQQVVFSMSFV
QGEESNDKIPVALGLKEKNLYLSCVLKDDKPTLQLESVDPKNYPKKKME
KRFVFNKIEINNKLEFESAQFPNWYISTSQAENMPVFLGGTKGGQDITDFTMQFVSS
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 :
TARC MouseDescription:
Thymus and Activation Regulated Chemokine (CCL17) Mouse Recombinant
C-C motif chemokine 17, Small-inducible cytokine A17, Thymus and activation-regulated chemokine, CC chemokine TARC, ABCD-2, CCL17, CCL-17, SCYA17, TARC, A-152E5.3, MGC138271, MGC138273.
Product # :
CHM-270Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TARC Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 70 amino acids and having a molecular mass of 7.9kDa. The TARC Mouse 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
The ED50 as determined by its ability to chemoattract BaF3 mouse pro-B cells transfected with human CCR4 is typically 2-10 ng/ml.More Info
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Introduction
TARC cDNA encodes a 94 amino acid precursor protein with a 23 amino acid residue signal peptide that is cleaved off to generate the 71 amino acid residue mature secreted protein. Along with CC chemokine family members, CCL-17 has approximately 24-29% amino acid sequence identity with RANTES, MIP-1a, MIP-1b, MCP-1, MCP-2, MCP-3 and I-309. TARC is expressed in thymus, and at a lower level in the lung, colon, and small intestine. TARC is in addition transiently expressed in stimulated peripheral blood mononuclear cells. Recombinant TARC has been shown to be chemotactic for T cell lines but not monocytes or neutrophils. CCL-17 was recently identified to be a specific functional ligand for CCR4, a receptor that is selectively expressed on T cells. CCL17 is one of quite a few Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. CCL17 shows chemotactic activity for T lymphocytes, but not monocytes or granulocytes. CCL17 binds to chemokine receptors CCR4 and CCR8. This chemokine plays important roles in T cell development in thymus as well as in trafficking and activation of mature T cells.
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Synonyms
C-C motif chemokine 17, Small-inducible cytokine A17, Thymus and activation-regulated chemokine, CC chemokine TARC, ABCD-2, CCL17, CCL-17, SCYA17, TARC, A-152E5.3, MGC138271, MGC138273.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TARC although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TARC should be stored at 4C between 2-7 days and for future use below -18C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized TARC 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
ARATNVGREC CLDYFKGAIP IRKLVSWYKT SVECSRDAIV FLTVQGKLIC ADPKDKHVKK AIRLVKNPRP.
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 :
CD11b Antibody, BiotinDescription:
CD11b, Mouse Anti-Human, Biotin
Integrin alpha-M, Cell surface glycoprotein MAC-1 subunit alpha, CR-3 alpha chain, Leukocyte adhesion receptor MO1, Neutrophil adherence receptor, CD11b antigen, ITGAM, CR3A, MO1A, CD11B, MAC-1, MAC1A, MGC117044.
Product # :
ANT-275Price :
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
Integrins are heterodimeric integral membrane proteins consisting of an ? chain and a ? chain. CD11b is an I-domain including ? integrin combines with the ? 2 chain (ITGB2) to form a leukocyte-specific integrin referred to as macrophage receptor also called MAC1. The ? M beta 2 integrin is crucial in the adherence of neutrophils and monocytes to stimulated endothelium, and also in the phagocytosis of complement coated particles. Multiple transcript variants encoding different isoforms have been found for this gene.
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Synonyms
Integrin alpha-M, Cell surface glycoprotein MAC-1 subunit alpha, CR-3 alpha chain, Leukocyte adhesion receptor MO1, Neutrophil adherence receptor, CD11b antigen, ITGAM, CR3A, MO1A, CD11B, MAC-1, MAC1A, MGC117044.
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Solubility
Reconstitute with of H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
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Immunogen
Purified human PBL Monocytes.
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Ig Subclass
Mouse IgG1.
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Clone
hCD11b.
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Applications
Blocking and staining antibody. For staining, use 10µl/1,000,000 cells. Titer for blocking LPS binding should be determined by the investigator.
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Available Conjugates
This antibody is also available unconjugated and conjugated to FITC. For staining with biotin or FITC-conjugated antibody use 5-10µl/1,000,000 cells.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
Lyophilized: store at 4°C. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
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Purification Method
Ion exchange column.
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 :
CRYGD MouseDescription:
Crystallin, Gamma D Mouse Recombinant
Gamma-crystallin D, Gamma-D-crystallin , Gamma-crystallin 1, CRYGD.
Product # :
PRO-2484Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CRYGD Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (1-174 a.a.) and having a molecular mass of 23.5kDa.CRYGD is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CRYGD protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
CRYGD is a member of the beta/gamma-crystallin family. Crystallins are the principal structural components of the vertebrate eye lens. The mammalian lens crystallins are divided into alpha, beta, and gamma families. Gamma-crystallins are involved in cataract formation. Defects in the CRYGD gene are responsible for cataract autosomal dominant (ADC), cataract congenital non-nuclear polymorphic autosomal dominant (CCP), cataract congenital cerulean type 3 (CCA3) and cataract crystalline aculeiform (CACA).
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Synonyms
Gamma-crystallin D, Gamma-D-crystallin , Gamma-crystallin 1, CRYGD.
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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 MGSMGKITFY EDRGFQGRHY ECSTDHSNLQ PYFSRCNSVR VDSGCWMLYE QPNFTGCQYF LRRGDYPDYQ QWMGFSDSVR SCRLIPHAGS HRIRLYEREE YRGQMIEFTE DCPSLQDRFH FNEIYSLNVL EGCWVLYDMT NYRGRQYLLR PGEYRRYHDW
GAMNARVGSL RRVMDFY
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 :
KLF4 Human, HisDescription:
Kruppel-Like Factor 4 Human Recombinant, His Tag
Kruppel-Like Factor 4 (Gut), GKLF, EZF, Epithelial Zinc Finger Protein EZF, Gut-Enriched Krueppel-Like Factor, Endothelial Kruppel-Like Zinc Finger Protein, Krueppel-Like Factor 4, Krueppel-like factor 4, Epithelial zinc finger protein EZF, Gut-enriched krueppel-like factor.
Product # :
PRO-2186Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KLF4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 422 amino acids (11-395 a.a) and having a molecular mass of 44.2kDa. KLF4 is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
KLF4 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
KLF4 is a transcription factor that performs as both an activator and repressor. KLF4 is expressed mainly in erythroid tissues and found mostly in gut. KLF4 is takes part in the differentiation of epithelial cells in addition to skeletal and kidney development.
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Synonyms
Kruppel-Like Factor 4 (Gut), GKLF, EZF, Epithelial Zinc Finger Protein EZF, Gut-Enriched Krueppel-Like Factor, Endothelial Kruppel-Like Zinc Finger Protein, Krueppel-Like Factor 4, Krueppel-like factor 4, Epithelial zinc finger protein EZF, Gut-enriched krueppel-like factor.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMAVS DALLPSFSTF ASGPAGREKT LRQAGAPNNR WREELSHMKR LPPVLPGRPY DLAAATVATD LESGGAGAAC GGSNLAPLPR RETEEFNDLL DLDFILSNSL THPPESVAAT VSSSASASSS SSPSSSGPAS APSTCSFTYP IRAGNDPGVA PGGTGGGLLY GRESAPPPTA PFNLADINDV SPSGGFVAEL LRPELDPVYI PPQQPQPPGG GLMGKFVLKA SLSAPGSEYG SPSVISVSKG SPDGSHPVVV APYNGGPPRT CPKIKQEAVS SCTHLGAGPP LSNGHRPAAH DFPLGRQLPS RTTPTLGLEE VLSSRDCHPA LPLPPGFHPH PGPNYPSFLP DQMQPQVPPL HYQELMPPGS CMPEEPKPKR GRRSWPRKRT AT.
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 :
LCN2 MouseDescription:
Neutrophil Gelatinase Associated Lipocalin/Lipocalin-2 Mouse Recombinant
Neutrophil gelatinase-associated lipocalin, NGAL, Lipocalin-2, SV-40-induced 24P3 protein, Siderocalin LCN2, p25.
Product # :
ENZ-875Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LCN2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 203 amino acids (21-200 a.a) and having a molecular mass of 23.3kDa. LCN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LCN2 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Lipocalin-2 also called Neutrophil Gelatinase Associated Lipocalin (NGAL) belongs to a family of lipocans which include 25 proteins (including a1-microglobulin and b-lactoglobulin), which are characterized by their ability to bind small lipophilic substances in their hydrophobic core.
They thereby serve as transporters of substances like retinal, biliverdins & prostaglandins. There are indications that NGAL is involved in modulation of the inflammatory response and is found in the plasma of patients after stroke. -
Synonyms
Neutrophil gelatinase-associated lipocalin, NGAL, Lipocalin-2, SV-40-induced 24P3 protein, Siderocalin LCN2, p25.
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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 MGSQDSTQNL IPAPSLLTVP LQPDFRSDQF RGRWYVVGLA GNAVQKKTEG SFTMYSTIYE LQENNSYNVT SILVRDQDQG CRYWIRTFVP SSRAGQFTLG NMHRYPQVQS YNVQVATTDY NQFAMVFFRK TSENKQYFKI TLYGRTKELS PELKERFTRF AKSLGLKDDN IIFSVPTDQC IDN.
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 :
TNFR MouseDescription:
Tumor Necrosis Factor Receptor Mouse Recombinant
Tumor necrosis factor receptor superfamily member 1A, Tumor necrosis factor receptor 1, TNF-R1, Tumor necrosis factor receptor type I, TNF-RI, TNFR-I, p55, p60, CD120a, Tnfrsf1a, Tnfr-1, Tnfr1, FPF, TNF-R, TNFAR, TNFRI, p55-R, TNFR60, Tnfr-2, TNF-R-I, TNF-R55, TNFRp55, TNF-alphaR1, TNFalpha-R1.
Product # :
CYT-774Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
TNFR Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 191 amino acids and having a molecular mass of 21.1kDa.The TNFR is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TNFR protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by its ability to inhibit the TNF-α mediated cytotoxicity in the L-929 cells is less than 1.0 µg/ml, corresponding to a specific activity of > 1000 IU/mg in the presence of 0.1 ng/mL of rMuTNF-a.More Info
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Introduction
TNFR1 belongs to the TNF-receptor superfamily. TNFR1 is a receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha.
There are 2 types of soluble TNF receptors: sTNFR-I and sTNFR-II, which act to neutralize the biological activities of TNF alpha and TNF beta. The levels of these soluble receptors seem to increase as a result of shedding of the extracellular domains of the membrane bound receptors. TNF-a, TNFR1 and TNFR2 have roles in cellular differentiation. TNFR1 and TNFR2 function in cell type-specific renal injury.
TNFR1 is capable of signaling both cell survival and apoptosis. TNFR1-induced apoptosis requires 2 sequential signaling complexes. TNFR1 is capable of activating NF-kappaB, mediate apoptosis, and function as a regulator of inflammation. Oxidative stress promotes TNFR1 and TNFR2 self-interaction, ligand-independent and enhanced ligand-dependent TNF signaling. TNFR1 contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase. Human TNFR1 has a major region which controls cell surface expression. High levels of soluble TNF receptors are found in the amniotic fluid of pregnant women.
Germline mutations of the extracellular domains of TNFR1 are linked to the autosomal dominant periodic fever syndrome. The impaired receptor clearance is believed to be a mechanism of the disease. Familial hibernian fever (FHF) is caused by defects in TNFRSF1A gene. -
Synonyms
Tumor necrosis factor receptor superfamily member 1A, Tumor necrosis factor receptor 1, TNF-R1, Tumor necrosis factor receptor type I, TNF-RI, TNFR-I, p55, p60, CD120a, Tnfrsf1a, Tnfr-1, Tnfr1, FPF, TNF-R, TNFAR, TNFRI, p55-R, TNFR60, Tnfr-2, TNF-R-I, TNF-R55, TNFRp55, TNF-alphaR1, TNFalpha-R1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TNFR although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TNFR should be stored at 4C between 2-7 days and for future use below -18C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized TNFR 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
IHPSGVTGLV PSLGDREKRD SLCPQGKYVH SKNNSICCTK CHKGTYLVSD CPSPGRDTVC RECEKGTFTA SQNYLRQCLS CKTCRKEMSQ VEISPCQADK DTVCGCKENQ FQRYLSETHF QCVDCSPCFN GTVTIPCKET QNTVCNCHAG FFLRESECVP CSHCKKNEEC MKLCLPPPLA NVTNPQDSGT 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 :
CD46 HumanDescription:
CD46 Human Recombinant
AHUS2, MCP, MIC10, TLX, TRA2.10, Membrane cofactor protein, Trophoblast leukocyte common antigen, CD46.
Product # :
PRO-1414Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CD46 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (35-313 a.a) and having a molecular mass of 33.8kDa. CD46 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CD46 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Membrane cofactor protein isoform 14 (CD46), is a type I membrane protein which has cofactor activity for inactivation of complement components C3b and C4b by serum factor I. This function resides in the complement control protein repeats (CCPs), with CCP1–4 vital for regulation. CD46 is also involved in the fusion of the spermatozoa with the oocyte during fertilization. CD46 is common in thymocytes, T cells, B cells, monocytes, granulocytes, NK cells, platelets, endothelial cells, epithelial cells, fibroblasts, placenta and sperm.
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Synonyms
AHUS2, MCP, MIC10, TLX, TRA2.10, Membrane cofactor protein, Trophoblast leukocyte common antigen, CD46.
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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 MGSCEEPPTF EAMELIGKPK PYYEIGERVD YKCKKGYFYI PPLATHTICD RNHTWLPVSD DACYRETCPY IRDPLNGQAV PANGTYEFGY QMHFICNEGY YLIGEEILYC ELKGSVAIWS GKPPICEKVL CTPPPKIKNG KHTFSEVEVF EYLDAVTYSC DPAPGPDPFS LIGESTIYCG DNSVWSRAAP ECKVVKCRFP VVENGKQISG FGKKFYYKAT VMFECDKGFY LDGSDTIVCD SNSTWDPPVP KCLKGPRPTY KPPVSNYPGY PKPEEGILDS LD.
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 :
BMP 7 Human, HEKDescription:
Bone Morphogenetic protein-7 Human Recombinant, HEK
Osteogenic Protein 1, BMP-7.
Product # :
CYT-082Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
BMP-7 Human Recombinant produced in HEK cells is a glycosylated disulfide-linked homodimer, having a molecular weight range of 30-38kDa due to glycosylation.The BMP7 corresponds to amino acid residues 315 to 431 of the full-length BMP-7 precursor and is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
The BMP7 was lyophilized from 1mg/ml in 1xPBS.
Purity
Greater than 95% as obsereved by SDS-PAGE.
Biological Activity
The specific activity was determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line (Mouse chondrogenic cell line) and is typically 50-250ng/ml.More Info
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Introduction
The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.
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Synonyms
Osteogenic Protein 1, BMP-7.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BMP7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-7 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 BMP-7 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
DFSLDNEVHSSFIHRRLRSQERREMQREILSILGLPHRPRPHLQGKHNSAPMFMLDLYNAM AVEEGGGPGGQGFSYPYKAVFSTQGPPLASLQDSHFLTDADMVMSFVNLVEHDKEFFHPR YHHREFRFDLSKIPEGEAVTAAEFRIYKDYIRERFDNETFRISVYQVLQEHLGRESDLFLDSRTLWASE EGWLVFDITATSNHWVVNPRHNLGLQLSVETLDGQSINPKLAGLIGRHGPQNKQPFMVAFFKAT.
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Background
BMP-7 Bone Morphogenetic Protein-7 Human Recombinant: A Key Regulator of Osteogenesis and Beyond
Abstract:
BMP-7 (Bone Morphogenetic Protein-7), also known as Osteogenic Protein 1 or BMP-7, is a potent growth factor that plays a crucial role in various biological processes, particularly in osteogenesis and tissue regeneration.
This research paper aims to comprehensively explore the molecular characteristics, signaling pathways, and diverse physiological functions of BMP-7.
Additionally, it investigates the therapeutic implications of BMP-7 in different disorders. Synonyms such as Osteogenic Protein 1 and BMP-7 associated with the protein are discussed throughout the paper to highlight their relevance in scientific literature.
Introduction:
BMP-7, also known as Osteogenic Protein 1 or BMP-7, is a growth factor with multifaceted roles in osteogenesis, tissue regeneration, and disease. This section introduces BMP-7 and its synonyms, highlighting their significance and relevance in scientific research.
Molecular Characteristics of BMP-7:
This section explores the molecular characteristics of BMP-7, including its primary amino acid sequence, protein structure, post-translational modifications, and binding partners. The importance of these factors in determining BMP-7's biological activity and receptor specificity is discussed.
Signaling Pathways Activated by BMP-7 :
BMP-7 activates specific signaling pathways upon binding to its receptors, leading to diverse cellular responses. This section focuses on the canonical BMP signaling pathway, highlighting the activation of Smad-dependent and Smad-independent pathways. The downstream effectors and transcriptional regulators involved in mediating BMP-7's cellular responses are also discussed.
Physiological Functions of BMP-7 :
BMP-7 plays critical roles in various physiological processes, particularly in osteogenesis and tissue regeneration. This section provides an in-depth analysis of BMP-7's contributions to these processes, emphasizing its role in promoting bone formation, cartilage development, renal function, and wound healing.
Therapeutic Implications of BMP-7 :
The unique properties of BMP-7 make it a promising therapeutic candidate for various disorders. This section discusses the potential applications of BMP-7 in bone regeneration, cartilage repair, kidney disease, and tissue engineering. The challenges and future directions in utilizing BMP-7 as a therapeutic agent are also explored.
BMP-7 in Disease Progression:
BMP-7 is implicated in the progression of certain diseases, including fibrosis, cancer, and cardiovascular disorders. This section examines the role of BMP-7 in tissue fibrosis, tumor progression, angiogenesis, and cardiac remodeling. The therapeutic implications and targeting of BMP-7 in disease management are also discussed.
Conclusion:
BMP-7, also known as Osteogenic Protein 1 or BMP-7, is a critical growth factor involved in osteogenesis, tissue regeneration, and disease progression. Understanding the molecular characteristics, signaling pathways, and physiological functions of BMP-7 contributes to the exploration of its therapeutic potential in various disorders.
What is the molecular weight/Mw of BMP7 Protein?
BMP7 Protein has a total Mw of 38kDa.
What is the source or expression system of BMP7 Protein?
HEK.
What is the Purity of BMP7 Protein?
BMP7 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMP7 Protein?
The specific activity was determined by the dose dependent induction of alkaline phosphatase production in the ATDC-5 cell line (Mouse chondrogenic cell line) and is typically 50-250ng/ml.
What is the amino acid sequence of BMP7 Protein?
DFSLDNEVHSSFIHRRLRSQERREMQREILSILGLPHRPRPHLQGKHNSAPMFMLDLYNAM AVEEGGGPGGQGFSYPYKAVFSTQGPPLASLQDSHFLTDADMVMSFVNLVEHDKEFFHPR YHHREFRFDLSKIPEGEAVTAAEFRIYKDYIRERFDNETFRISVYQVLQEHLGRESDLFLDSRTLWASE EGWLVFDITATSNHWVVNPRHNLGLQLSVETLDGQSINPKLAGLIGRHGPQNKQPFMVAFFKAT.
What applications can BMP7 Protein be used in?
BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMP7 Protein?
The endotoxin level is minimal, BMP7 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CD96 HumanDescription:
CD96 Human Recombinant
CD96 Molecule, T Cell-Activated Increased Late Expression Protein, Cell Surface Antigen CD96, CD96 Antigen, T Cell Activation, Increased Late Expression, T-Cell Surface Protein Tactile, TACTILE.
Product # :
PRO-2445Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CD96 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 490 amino acids (22-503a.a.) and having a molecular mass of 54.6kDa.CD96 is expressed with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CD96 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CD96 is a type I membrane protein which is a part of the immunoglobulin superfamily. CD96 functions as cell markers in immune-phynotyping and participates in antigen presentation. CD96 plays a role in the adhesive interactions of activated T and NK cells through the late phase of the immune response.
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Synonyms
CD96 Molecule, T Cell-Activated Increased Late Expression Protein, Cell Surface Antigen CD96, CD96 Antigen, T Cell Activation, Increased Late Expression, T-Cell Surface Protein Tactile, TACTILE.
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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
VWEKTVNTEE NVYATLGSDV NLTCQTQTVG FFVQMQWSKV TNKIDLIAVY HPQYGFYCAY GRPCESLVTF TETPENGSKW TLHLRNMSCS VSGRYECMLV LYPEGIQTKI YNLLIQTHVT ADEWNSNHTI EIEINQTLEI PCFQNSSSKI SSEFTYAWSV EDNGTQETLI SQNHLISNST LLKDRVKLGT DYRLHLSPVQ IFDDGRKFSC HIRVGPNKIL RSSTTVKVFA KPEIPVIVEN NSTDVLVERR FTCLLKNVFP KANITWFIDG SFLHDEKEGI YITNEERKGK DGFLELKSVL TRVHSNKPAQ SDNLTIWCMA LSPVPGNKVW NISSEKITFL LGSEISSTDP PLSVTESTLD TQPSPASSVS PARYPATSSV TLVDVSALRP NTTPQPSNSS MTTRGFNYPW TSSGTDTKKS VSRIPSETYS SSPSGAGSTL HDNVFTSTAR AFSEVPTTAN GSTKTNHVHI TGIVVNKPKD GMLEHHHHHH.
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 :
SRGN HumanDescription:
Serglycin Human Recombinant
Serglycin, PRG, PRG1, PPG, Proteoglycan 1 secretory granule, Hematopoetic proteoglycan core protein, Platelet proteoglycan core protein, proteoglycan protein core for mast cell secretory granule.
Product # :
PRO-965Price :
Quantity :
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Description
SRGN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (28-158) and having a molecular mass of 17.4 kDa (Molecular weight on SDS-PAGE will appear higher).SRGN is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The SRGN solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.15M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
SRGN is identified as a hematopoietic cell granule proteoglycan. Proteoglycans stored in the secretory granules of various hematopoietic cells also hold a protease-resistant peptide core, and is vital for neutralizing hydrolytic enzymes. SRGN is related to the macromolecular complex of granzymes and perforin that acts as a intermediary of granule-mediated apoptosis.
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Synonyms
Serglycin, PRG, PRG1, PPG, Proteoglycan 1 secretory granule, Hematopoetic proteoglycan core protein, Platelet proteoglycan core protein, proteoglycan protein core for mast cell secretory granule.
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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 MGSHMYPTRR ARYQWVRCNP DSNSANCLEE KGPMFELLPG ESNKIPRLRT DLFPKTRIQD LNRIFPLSED YSGSGFGSGS GSGSGSGSGF LTEMEQDYQL VDESDAFHDN LRSLDRNLPS DSQDLGQHGL EEDFML.
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 :
IFN a 2a HumanDescription:
IFN-Alpha 2a Human Recombinant
Leukocyte IFN, B cell IFN, Type I IFN, IFNA2, IFN-a 2a, Interferon-alpha-2a.
Product # :
CYT-204Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IFN Alpha Human 2a Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 19241 Dalton. The difference between IFNA2A and IFNA2B is in the amino acid present at position 23. IFN-alpha 2a has a lysine at that position 23 while IFN-alpha 2b has arginine.The Interferon-alpha-2a gene was obtained from human leukocytes.The IFNA2A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized without additives.
Purity
Greater than 97.0% as determined by both:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 270,000,000 IU/mg.More Info
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Introduction
IFN-alpha is produced by macrophages and has antiviral activities. IFN stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.
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Synonyms
Leukocyte IFN, B cell IFN, Type I IFN, IFNA2, IFN-a 2a, Interferon-alpha-2a.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IFNA-2A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-alpha 2a 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 Interferon-alpha-2a 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
CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEM IQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAV RKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE.
N-terminal methionine has been completely removed enzymatically.
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Background
What is the molecular weight/Mw of IFN A 2A HUMAN Protein?
IFN A 2A HUMAN Protein has a total Mw of 19.2kDa.
What is the source or expression system of IFN A 2A HUMAN Protein?
Escherichia Coli.
What is the Purity of IFN A 2A HUMAN Protein?
IFN A 2A HUMAN Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of IFN A 2A HUMAN Protein?
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 270,000,000 IU/mg.
What is the amino acid sequence of IFN A 2A HUMAN Protein?
CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEM IQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAV RKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE.
N-terminal methionine has been completely removed enzymatically.
What applications can IFN A 2A HUMAN Protein be used in?
IFN A 2A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFN A 2A HUMAN Protein?
The endotoxin level is minimal, IFN A 2A HUMAN Protein was purified using conventional chromatography techniques.
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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 0.924 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 IFN-a 2a 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 :
IP 10 Human, HisDescription:
IP-10 Human Recombinant (CXCL10), His Tag
Small inducible cytokine B10, CXCL10, 10 kDa interferon-gamma-induced protein, Gamma-IP10, IP-10, chemokine (C-X-C motif) ligand 10, C7, IFI10, INP10, crg-2, mob-1, SCYB10, gIP-10.
Product # :
CHM-346Price :
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Shipped with Ice Packs
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Description
IP-10 His Tag Human Recombinant ?produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 77 amino acids fragment (22-98) and having a total molecular mass of 8.5 kDa with an amino-terminal hexahistidine tag. The IP-10 His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IP-10 His is supplied in 10mM Tris HCl pH8, 1mM EDTA and 50% glycerol.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Chemokine (C-X-C motif) ligand 10 (CXCL10) is a small cytokine belonging to the CXC chemokine family that is also known as 10 kDa interferon-gamma-induced protein (?-IP10 or IP-10). CXCL10 is secreted by several cell types in response to IFN-?. These cell types include monocytes, endothelial cellsand fibroblasts. CXCL10 has been attributed to several roles, such as chemoattraction for monocytesand T cells, promotion of T cell adhesion to endothelial cells, anti tumor activity, and inhibition of bone marrow colony formation and angiogenesis. The gene for CXCL10 is located on human chromosome 4in a cluster among several other CXC chemokines. This chemokine elicits its effects by binding to the cell surface chemokine receptor CXCR3. The three-dimensional crystal structure of this chemokine has been determined under 3 different conditions to a resolution of up to 1.92A.
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Synonyms
Small inducible cytokine B10, CXCL10, 10 kDa interferon-gamma-induced protein, Gamma-IP10, IP-10, chemokine (C-X-C motif) ligand 10, C7, IFI10, INP10, crg-2, mob-1, SCYB10, gIP-10.
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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 :
HCST HumanDescription:
Hematopoietic Cell Signal Transducer Human Recombinant
Hematopoietic Cell Signal Transducer, DNAX-Activation Protein 10, Phosphoinositide-3-Kinase Adaptor Protein, Transmembrane Adapter Protein KAP10, Kinase Assoc Pro Of ~10kDa, Membrane Protein DAP10, PIK3AP, DAP10, KAP10, Kinase Assoc Protein.
Product # :
PRO-2522Price :
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Shipped with Ice Packs
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Description
HCST produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 271 amino acids (20-48 a.a.) and having a molecular mass of 30.1kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).HCST is expressed with a 242 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
HCST protein solution (1mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
HCST (Hematopoietic Cell Signal Transducer) is part of the DAP10 family. HCST is capable of being a part of an immunoreceptor complex. HCST takes a vital part in inducing cytotoxicity against MHC class I chain-associated MICA & target cells expressing cell surface ligands such as UL16-binding protein (ULBP) & MICB. HCST complex participates in proliferation as well as cell survival by activating T & NK cell responses.
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Synonyms
Hematopoietic Cell Signal Transducer, DNAX-Activation Protein 10, Phosphoinositide-3-Kinase Adaptor Protein, Transmembrane Adapter Protein KAP10, Kinase Assoc Pro Of ~10kDa, Membrane Protein DAP10, PIK3AP, DAP10, KAP10, Kinase Assoc Protein.
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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
ADPTTPGERS SLPAFYPGTS GSCSGCGSLS LPLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NTRK2 Human , HEKDescription:
Neurotrophic Receptor Tyrosine Kinase 2, HEK Human Recombinant
GP145-TrkB, trk-B, TRKB, NTRK2.
Product # :
CYT-1230Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NTRK2 Human Recombinant is a single, glycosylated, polypeptide chain (32-430 a.a) containing a total of 632 amino acids and having a molecular mass of 70.3 kDa. NTRK2 is fused to a 233 a.a hIgG-His-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The NTRK2 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Synonyms
GP145-TrkB, trk-B, TRKB, NTRK2.
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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
CPTSCKCSAS RIWCSDPSPG IVAFPRLEPN SVDPENITEI FIANQKRLEI INEDDVEAYV GLRNLTIVDS GLKFVAHKAF LKNSNLQHIN FTRNKLTSLS RKHFRHLDLS ELILVGNPFT CSCDIMWIKT LQEAKSSPDT QDLYCLNESS KNIPLANLQI PNCGLPSANL AAPNLTVEEG KSITLSCSVA GDPVPNMYWD VGNLVSKHMN ETSHTQGSLR ITNISSDDSG KQISCVAENL VGEDQDSVNL TVHFAPTITF LESPTSDHHW CIPFTVKGNP KPALQWFYNG AILNESKYIC TKIHVTNHTE YHGCLQLDNP THMNNGDYTL IAKNEYGKDE KQISAHFMGW PGIDDGANPN YPDVIYEDYG TAANDIGDTT NRSNEIPSTD VTDKTGREH LEPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GK.
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Background
NTRK2, also known as TrkB, is a high-affinity receptor for BDNF and other neurotrophins such as neurotrophin-4 (NT-4) and neurotrophin-3 (NT-3). It plays a crucial role in the development, function, and plasticity of the nervous system. Dysregulation of NTRK2 signaling is associated with various neurological disorders, including neurodegenerative diseases, psychiatric disorders, and cancers. NTRK2 has been developed to facilitate research into its biological functions and potential therapeutic applications. This paper provides a comprehensive overview of the scientific research on recombinant human NTRK2, focusing on its biological functionality, detailed description, and physical properties.
NTRK2 is critical for synaptic plasticity, which underlies learning and memory. Research with rhNTRK2 has demonstrated that BDNF-NTRK2 signaling enhances synaptic strength and facilitates long-term potentiation (LTP) in hippocampal neuron.
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 :
EGF Mouse, HisDescription:
Epidermal Growth Factor Mouse Recombinant, His Tag
Urogastrone, URG, EGF.
Product # :
CYT-138Price :
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Shipped with Ice Packs
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- SDS-PAGE
Description
EGF mouse Recombinant produced in E. coli is a single polypeptide chain containing 77 amino acids (977-1029) and having a molecular mass of 8.6kDa.EGF is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The EGF solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 2mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
SDS-PAGE
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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. -
Synonyms
Urogastrone, URG, EGF.
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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 MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.
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Background
Unveiling Epidermal Growth Factor Mouse Recombinant: Harnessing His Tag for Enhanced Insights and Therapeutic Prospects
Abstract:
This research paper delves into the realm of Epidermal Growth Factor Mouse Recombinant (EGF-MR), focusing on the strategic integration of a Histidine (His) Tag. By employing sophisticated methodologies encompassing protein engineering, chromatographic techniques, and cellular assays, this study unveils the multifaceted molecular attributes of EGF-MR with His Tag. The findings not only enhance our understanding of EGF-MR's behavior but also illuminate potential avenues for therapeutic interventions.
Introduction:
Epidermal Growth Factor (EGF) governs vital cellular processes. This paper delves into Epidermal Growth Factor Mouse Recombinant (EGF-MR) with a specific emphasis on the incorporation of a Histidine (His) Tag, unraveling its molecular intricacies and therapeutic implications.
Protein Engineering and His Tag Integration:
The paper navigates the tailored engineering of EGF-MR to accommodate a His Tag, a peptide sequence that facilitates protein purification. The process involves strategic modification of the EGF-MR gene to ensure proper folding and presentation of the His Tag.
Chromatographic Purification and His Tag Affinity:
Chromatographic techniques, specifically immobilized metal ion affinity chromatography (IMAC), are employed to purify the His-tagged EGF-MR. The His Tag's high affinity for metal ions facilitates efficient purification, yielding a highly purified and bioactive protein product.
Structural and Functional Insights:
The presence of the His Tag is not just for purification; it serves as a molecular handle to investigate EGF-MR's structural dynamics. High-resolution structural analyses coupled with biophysical assays unravel how the His Tag affects EGF-MR's conformation and binding interactions.
Cellular Assays and Bioactivity Assessment:
In vitro cellular assays, including proliferation and migration studies, provide insights into the impact of His Tag on EGF-MR's bioactivity. Comparative analyses shed light on the functionality of His-tagged EGF-MR and its potential implications in cellular responses.
Therapeutic Prospects and Targeted Delivery:
The incorporation of a His Tag presents a unique avenue for tailored drug delivery. The His Tag can serve as a docking site for targeted therapies, enabling precise interactions with specific receptors on target cells.
Future Directions and Challenges:
While promising, challenges such as potential steric hindrance from the His Tag require consideration. Future research should focus on optimizing the positioning of the His Tag to maintain EGF-MR's full biological activity.
Conclusion:
In a harmonious synthesis of advanced methodologies and innovative insights, the integration of His Tag into Epidermal Growth Factor Mouse Recombinant emerges as a transformative paradigm. The His Tag not only facilitates purification but also offers a molecular window into EGF-MR's behavior, potentially redefining targeted therapies and precision medicine.
What is the molecular weight/Mw of EGF MOUSE, HIS Protein?
EGF MOUSE, HIS Protein has a total Mw of 8.6kDa.
What is the source or expression system of EGF MOUSE, HIS Protein?
Escherichia Coli.
What is the Purity of EGF MOUSE, HIS Protein?
EGF MOUSE, HIS Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of EGF MOUSE, HIS Protein?
The biological functionality of EGF MOUSE, HIS Protein will be determined in the future.
What is the amino acid sequence of EGF MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.
What applications can EGF MOUSE, HIS Protein be used in?
EGF MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EGF MOUSE, HIS Protein?
The endotoxin level is minimal, EGF 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.
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Name :
NRG1 B1 HumanDescription:
Neuregulin-1/Heregulin-b1 Human Recombinant
Neuregulin-1, Heregulin-b1, NRG1-B1, NRG1 B1.
Product # :
CYT-733Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
- source
- formulation
- purity
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Description
Recombinant Human Neuregulin-1/Heregulin-b1 produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 177-241) containing 65 amino acids and having a total molecular mass of 7.5kDa. NRG1-B1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered solution in 1×PBS, pH 7.4 and 5% trehalose.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 was determined by the dose-dependent stimulation of the proliferation of human MCF-7 cells is less than 0.5ng/ml, corresponding to a specific activity of >2.0×106 units/mg.More Info
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Introduction
Neuregulin/Heregulin is a family of structurally related polypeptide growth factors which are stemmed from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). Thus far, there are more than 14 soluble and transmembrane proteins derived from the NRG1 gene. Proteolytic processing of the extracellular domain of the transmembrane NRG1 isoforms release soluble growth factors. HRG1-b1 is comprised of an Ig domain and an EGF-like domain which is necessary for direct binding to receptor tyrosine kinases erb3 and erb4. This binding stimulates erb3 and erb4 heterodimerization with erb2, promoting intrinsic kinase activity, which results in tyrosine phosphorylation. Even though HRG1-b1 biological effects are still unclear, it has been discovered to advance motility and invasiveness of breast cancer cells which in addition might entail up-regulation of expression and function of the autocrine motility-promoting factor (AMF).
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Synonyms
Neuregulin-1, Heregulin-b1, NRG1-B1, NRG1 B1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized NRG1-B1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NRG1-B1 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 NRG1-B1 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
SHLVKCAEKE KTFCVNGGEC FMVKDLSNPS RYLCKCPNEF TGDRCQNYVM ASFYKHLGIE FMEAE.
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 :
OPG Human, Hi-5Description:
Osteoprotegerin Human Recombinant, Hi-5
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, Osteoprotegerin, TR1, MGC29565.
Product # :
CYT-633Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Osteoprotegerin produced in baculovirus is a signle, glycosylated polypeptide chain containing 389 amino acid residues (22-401 a.a.), having a calculated molecular mass of 44.7 kDa. The Osteoprotegerin is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Hi-5.
Formulation
Osteoprotegerin protein contains PBS pH-7.4 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range ≤ 8 ng/ml and is measured by its ability to inhibit cytotoxicity using Jurkat human acute T cell leukemia cells in the presence of 2ng/ml of human TRAIL (CAT# cyt-1014).
More Info
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Introduction
Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.
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Synonyms
TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, Osteoprotegerin, TR1, MGC29565.
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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. Please avoid freeze thaw cycles.
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Amino Acid Sequence
ADPETFPPKY LHYDEETSHQ LLCDKCPPGT YLKQHCTAKW KTVCAPCPDH YYTDSWHTSD ECLYCSPVCK ELQYVKQECN RTHNRVCECK EGRYLEIEFC LKHRSCPPGF GVVQAGTPER NTVCKRCPDG FFSNETSSKA PCRKHTNCSV FGLLLTQKGN ATHDNICSGN SESTQKCGID VTLCEEAFFR FAVPTKFTPN WLSVLVDNLP GTKVNAESVE RIKRQHSSQE QTFQLLKLWK HQNKDQDIVK KIIQDIDLCE NSVQRHIGHA NLTFEQLRSL MESLPGKKVG AEDIEKTIKA CKPSDQILKL LSLWRIKNGD QDTLKGLMHA LKHSKTYHFP KTVTQSLKKT IRFLHSFTMY KLYQKLFLEM IGNQVQSVKI SCLSHHHHHH.
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 :
KXD1 HumanDescription:
KxDL Motif Containing 1 Human Recombinant
C19orf50, KXDL, MST096, MSTP096, KXD1.
Product # :
PRO-1656Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KXD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids (1-176 a.a.) and having a molecular mass of 22.1kDa.KXD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
KXD1 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
KxDL Motif Containing 1 (KXD1) is a member of the KXD1 family. KXD1 is participating in endosomal cargo sorting. KXD1 contacts with the BLOC-1 complex and Interacts with BLOC1S1. KXD1 Interacts with DTNBP1/BLOC1S7 through coiled-coil domain.
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Synonyms
C19orf50, KXDL, MST096, MSTP096, KXD1.
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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 MGSMDLPDSA SRVFCGRILS MVNTDDVNAI ILAQKNMLDR FEKTNEMLLN FNNLSSARLQ QMSERFLHHT RTLVEMKRDL DSIFRRIRTL KGKLARQHPE AFSHIPEASF LEEEDEDPIP PSTTTTIATS EQSTGSCDTS PDTVSPSLSP GFEDLSHVQP GSPAINGRSQ TDDEEMTGE.
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 :
ADH1C Human, sf9Description:
Alcohol Dehydrogenase 1C, Human Recombinant, sf9
ADH1, ADH1C, ADH3, Alcohol dehydrogenase 1C, Alcohol dehydrogenase subunit gamma.
Product # :
ENZ-1010Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ADH1C Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 381 amino acids (1-375) and having a molecular mass of 40.6kDa. ADH1C is fused to a 6 amino acid IgG His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ADH1C protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
ADH1C is a member of the zinc-containing alcohol dehydrogenase family which metabolizes a large assortment of substrates, such as ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. ADH1 is a monomorphic and a key factor in fetal and infant livers, becoming less active in gestation and only weakly active during adulthood.
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Synonyms
ADH1, ADH1C, ADH3, Alcohol dehydrogenase 1C, Alcohol dehydrogenase subunit gamma.
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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
MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAAGICRSD EHVVSGNLVT PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLFTPQCGK CRICKNPESN YCLKNDLGNP RGTLQDGTRR FTCSGKPIHH FVGVSTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG YGSAVKVAKV TPGSTCAVFG LGGVGLSVVM GCKAAGAARI IAVDINKDKF AKAKELGATE CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ NLSINPMLLL TGRTWKGAIF GGFKSKESVP KLVADFMAKK FSLDALITNI LPFEKINEGF DLLRSGKSIR
TVLTFHHHHH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CSK AntibodyDescription:
C-Src Tyrosine Kinase, Mouse Anti Human
Tyrosine-protein kinase CSK, C-Src kinase, Protein-tyrosine kinase CYL, CSK, C-Src Tyrosine Kinase.
Product # :
ANT-693Price :
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
C-Src Tyrosine Kinase, also known as CSK, regulates cell growth, migration, differentiation, and immune response. CSK Phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases. CSK is a protein coding gene which suppresses signaling by several surface receptors. Among CSK's related pathways are PI-3K cascade and Signaling by FGFR.
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Synonyms
Tyrosine-protein kinase CSK, C-Src kinase, Protein-tyrosine kinase CYL, CSK, C-Src Tyrosine Kinase.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human CSK mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CSK amino acids 1-450 purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
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Clone
PAT7C6AT.
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Applications
CSK antibody has been tested by ELISA, Western blot analysis and ICC/IF 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
CSK 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.