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261 results found for “signal recognition particle”
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Name :
CLEC7A HumanDescription:
C-Type Lectin Domain Family 7, Member A Human Recombinant
BGR, Dendritic Cell-Associated C-Type Lectin-1, Dendritic Cell-Associated C-Type Lectin 1, C-Type Lectin Domain Family 7, Member A, Lectin-Like Receptor 1, CD369 Antigen, CANDF4, SCARE2, CD369, C-Type Lectin Domain Containing 7A, C-Type Lectin Domain Family 7 Member A, C-Type (Calcium Dependent, Carbohydrate-Recognition Domain) Lectin, Superfamily Member 12, C-Type Lectin Superfamily Member 12, DC-Associated C-Type Lectin 1, Beta-Glucan Receptor, Dectin-1, CLECSF12, DECTIN1.
Product # :
PRO-2634Price :
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Shipped with Ice Packs
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Description
CLEC7A Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 183 amino acids (71-244 a.a) and having a molecular mass of 21kDa. CLEC7A is fused to a 9 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The CLEC7A solution (0.5mg/1ml) 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
C-type lectin domain family 7 member A 1 or CLEC7A is a protein, that in the innate immune system, acts against fungal pathogens. CLEC7A can be found in the immune system response cells such as monocytes, macrophages & neutrophils, or in dendritic and T cells. The protein is enhanced by macrophages by using GM-CSF, IL-4, or IL-13, or diminishes by dexamethasone, IL-10 and LPS.
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Synonyms
BGR, Dendritic Cell-Associated C-Type Lectin-1, Dendritic Cell-Associated C-Type Lectin 1, C-Type Lectin Domain Family 7, Member A, Lectin-Like Receptor 1, CD369 Antigen, CANDF4, SCARE2, CD369, C-Type Lectin Domain Containing 7A, C-Type Lectin Domain Family 7 Member A, C-Type (Calcium Dependent, Carbohydrate-Recognition Domain) Lectin, Superfamily Member 12, C-Type Lectin Superfamily Member 12, DC-Associated C-Type Lectin 1, Beta-Glucan Receptor, Dectin-1, CLECSF12, DECTIN1.
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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
ADPRHNSGRN PEEKDNFLSR NKENHKPTES SLDEKVAPSK ASQTTGGFSQ SCLPNWIMHG KSCYLFSFSG NSWYGSKRHC SQLGAHLLKI DNSKEFEFIE SQTSSHRINA FWIGLSRNQS EGPWFWEDGS AFFPNSFQVR NTVPQESLLH NCVWIHGSEV YNQICNTSSY SICEKELHHH HHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TNF a 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 :
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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 :
TNFSF12 HumanDescription:
TNF Ligand Superfamily Member 12 Human Recombinant
TWEAK, TNF-related weak inducer of apoptosis, TNFSF12, DR3LG, Apo3-Ligand, APO3L, TNFRSF12A, Tumor necrosis factor ligand superfamily member 12, MGC20669, MGC129581.
Product # :
CYT-699Price :
Quantity :
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Shipped at Room temp
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Description
TNFSF12 Human Recombinant (94-249 a.a.) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 156 amino acids and having a total molecular mass of 18kDa. The TNFSF12 is fused with an 8 amino acids his tag at N-terminal (M-HHHHHH-R, total 164 a.a.) and purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
Lyophilized from a 0.2μm filtered solution in PBS.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured in a proliferation assay using HUVECs, is less than 8ng/ml.
More Info
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Introduction
TNFSF12 is a cytokine that is part of the TNF ligand family. TNFSF12 is a ligand for the FN14/TWEAKR receptor. TNFSF12 has overlapping signaling functions with TNF, but displays a much wider tissue distribution. TNFSF12 induces apoptosis through multiple pathways of cell death in a cell type-specific manner. TNFSF12 promotes proliferation and migration of endothelial cells, and therefore acts as a regulator of angiogenesis. TNFSF12 is expressed in adult heart, pancreas, skeletal muscle, small intestine, spleen and peripheral blood lymphocytes. TWEAK h induces NFkB and chemokine secretion. TNFSF12 exerts an apoptotic activity in HT-29 human adenocarcinoma cells whilst cultured in the presence of IFN-?. TNFSF12 promotes proliferation and migration of endothelial cells.
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Synonyms
TWEAK, TNF-related weak inducer of apoptosis, TNFSF12, DR3LG, Apo3-Ligand, APO3L, TNFRSF12A, Tumor necrosis factor ligand superfamily member 12, MGC20669, MGC129581.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TNFSF12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TWEAK should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized TNFSF12 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MHHHHHHRSA PKGRKTRARR AIAAHYEVHP RPGQDGAQAG VDGTVSGWEE ARINSSSPLR YNRQIGEFIV TRAGLYYLYC QVHFDEGKAV YLKLDLLVDG VLALRCLEEF SATAASSLGP QLRLCQVSGL LALRPGSSLR IRTLPWAHLK AAPFLTYFGL FQVH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL 1RA HumanDescription:
Interleukin-1 Receptor Antagonist Human Recombinant
IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.
Product # :
CYT-203Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IL1ra Human Recombinant produced in E.Coli is a non-glycosylated, N-terminal methionyl form of the human naturally-occurring polypeptide chain containing 153 amino acids and having a molecular mass of 17000 Dalton. The IL1ra is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized protein with no additives.
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-dependant inhibition of IL-1 stimulation of D10S cells was found to be 0.5 ng/ml corresponding to a Specific Activity of 2,000,000IU/mg.More Info
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Introduction
Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.
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Synonyms
IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin 1ra although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1ra should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin-1 ra 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
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Arg-Pro-Ser-Gly.
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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 0.89 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-1 ra 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 :
sCD40L Mouse, sf9Description:
soluble CD40 Ligand/TRAPMouse Recombinant, sf9
CD40 ligand, T-cell antigen Gp39, TNF-related activation protein, TRAP, Tumor necrosis factor ligand superfamily member 5, CD154, CD40lg, CD154, CD40-L, Cd40l, gp39, HIGM1, IGM, IMD3, Ly-62, Ly62, T-BAM, Tnfsf5.
Product # :
CYT-917Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
sCD40 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 155 amino acids (112-260 a.a.) and having a molecular mass of 17.2kDa (Migrates at 18-28kDa on SDS-PAGE under reducing conditions).sCD40 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
sCD40 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
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 ligand, T-cell antigen Gp39, TNF-related activation protein, TRAP, Tumor necrosis factor ligand superfamily member 5, CD154, CD40lg, CD154, CD40-L, Cd40l, gp39, HIGM1, IGM, IMD3, Ly-62, Ly62, T-BAM, Tnfsf5.
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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
MQRGDEDPQI AAHVVSEANS NAASVLQWAK KGYYTMKSNL VMLENGKQLT VKREGLYYVY TQVTFCSNRE PSSQRPFIVG LWLKPSSGSE RILLKAANTH SSSQLCEQQS VHLGGVFELQ AGASVFVNVT EASQVIHRVG FSSFGLLKLH HHHHH.
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 :
SF20 HumanDescription:
MYDGF Human Recombinant
C19orf10, Interleukin-25, IL-25, IL25, IL27, IL-27, IL27w, IL-27w, Stromal cell-derived growth factor SF20, UPF0556 protein C19orf10, chromosome 19 open reading frame 10.
Product # :
CYT-622Price :
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Shipped with Ice Packs
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- sds-page
Description
SF20 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 162 amino acids fragment (33-173) and having a total molecular mass of 18 kDa. C9orf10 is fused to 20 amino acids His tag at N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
C9orf10 is supplied in 20mM Tris HCL pH-8 and 20% glycerol.
Purity
Greater than 95.0% by SDS-PAGE.
sds-page
More Info
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Introduction
SF20 plays a role in proliferation of lymphoid cells and is considered an interleukin. SF20 was initially identified as a product of bone marrow-derived stromal cells.
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Synonyms
C19orf10, Interleukin-25, IL-25, IL25, IL27, IL-27, IL27w, IL-27w, Stromal cell-derived growth factor SF20, UPF0556 protein C19orf10, chromosome 19 open reading frame 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 :
TNF a CanineDescription:
Tumor Necrosis Factor-Alpha Canine Recombinant
Tumor necrosis factor, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, TNFA, TNFSF2.
Product # :
CYT-140Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TNF-a Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 157 amino acids and having a molecular mass of 17.3 kDa. The TNF-a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 1×PBS, pH7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Specific Activity is >3.3×105 IU/mg as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D.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
Tumor necrosis factor, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, TNFA, TNFSF2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Tumor Necrosis Factor-a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNF-a should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Tumor Necrosis Factor-alpha in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
VKSSSRTPSD KPVAHVVANP EAEGQLQWLS RRANALLANG VELTDNQLIV PSDGLYLIYS QVLFKGQGCP STHVLLTHTI SRFAVSYQTK VNLLSAIKSP CQRETPEGTE AKPWYEPIYL GGVFQLEKGD RLSAEINLPN YLDFAESGQV YFGIIAL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TNF alpha humanDescription:
Tumor Necrosis Factor-Alpha Human Recombinant
TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.
Product # :
CYT-223Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Tumor Necrosis Factor-a Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids (157 a.a. of the mature human TNF-alpha and an N-terminal methionine) and having a molecular mass of 17.5kDa. The TNF-alpha is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
TNF-a Human was lyophilized from a concentrated 1mg/ml solution containing 20mM PB, pH-7.2, and 100mM NaCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Specific Activity is >5.0×107 IU/mg as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D.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, INS 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 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
MVRSSSRTPS DKPVAHVVAN PQAEGQLQWL NRRANALLAN GVELRDNQLV VPSEGLYLIY SQVLFKGQGC PSTHVLLTHT ISRIAVSYQT KVNLLSAIKS PCQRETPEGA E AKPWYEPIY LGGVFQLEKG DRLSAEINRP DYLDFAESGQ VYFGIIAL.
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Background
TNF Alpha Human: An Overview of Its Role and Importance in Immunology
TNF alpha human, also known as Tumor Necrosis Factor-alpha, is a critical cytokine in the immune system. Macrophages mainly produce this protein, and it plays a key role in inflammation and the acute phase reaction.
This protein is involved in various cellular functions, including cell death, differentiation, proliferation, and immune regulation.
Production and Properties
Tumor Necrosis Factor-alpha is produced recombinantly in E. coli and consists of a single, non-glycosylated polypeptide chain. It includes 157 amino acids of the mature human TNF-alpha and an N-terminal methionine, resulting in a molecular mass of approximately 17.5 kDa.
Furthermore, the protein is purified through standard chromatographic techniques to ensure high purity and biological activity.
Solubility and Usage
The lyophilized form of TNF appears as a sterile, white powder. It is recommended to reconstitute this powder in sterile water to achieve a solution of no less than 100µg/ml.
This solution can then be further diluted for various experimental applications. TNF alpha is used extensively in research, particularly for studying its effects on cell signaling and immune response.
Storage and Stability
For long-term storage, TNF should be kept desiccated below -18°C. Once reconstituted, it should be used within a week if stored at 4°C or kept below -18°C for future use. Avoiding freeze-thaw cycles is crucial to maintain the protein's functionality.
Biological Role and Implications
TNF alpha human is involved in the regulation of immune cells and is known for its role in inflammatory processes.
Dysregulation of TNF alpha production is linked to various diseases, such as autoimmune disorders, insulin resistance, and cancer. It is also a target for therapeutic interventions, particularly in conditions like rheumatoid arthritis and inflammatory bowel disease.
Mechanism of Action
TNF alpha can induce fever, apoptotic cell death, and can inhibit tumorigenesis and viral replication. Moreover, it is a potent mediator of the acute phase reaction, which influences the activity of various cells involved in systemic inflammation.
Research and Clinical Importance
Scientific research on TNF has provided insights into its complex role in disease mechanisms. Its interaction with receptors such as TNFRSF1A underscores its multifaceted effects across different organ systems, from liver function to brain activity.
Ongoing studies continue to explore its therapeutic potential, especially how it can be modulated to treat diseases without harmful side effects.
In essence, TNF alpha human is a versatile and powerful component of the immune system, important for both health and disease. Understanding its pathways and functions helps scientists develop better treatments for various inflammatory and autoimmune diseases.
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 :
CD38 HumanDescription:
CD38 Human Recombinant
P28907, ADP-Ribosyl Cyclase 1, 2-Phospho-Cyclic-ADP-Ribose Transferase, Cyclic ADP-Ribose Hydrolase, 2-Phospho-ADP-Ribosyl Cyclase, NAD(+) Nucleosidase, CD38 Antigen (P45), ADPRC 1, 2-Phospho-ADP-Ribosyl Cyclase/2-Phospho-Cyclic-ADP-Ribose Transferase, Ecto-Nicotinamide Adenine Dinucleotide Glycohydrolase , Cluster Of Differentiation 38, CADPr Hydrolase 1,CD38 Antigen, EC 2.4.99.20, EC 3.2.2.6, ADPRC1, T10.
Product # :
PRO-2320Price :
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Description
CD38 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 269 amino acids (43-300 a.a.) and having a molecular mass of 31.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). CD38 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CD38 protein solution (1mg/ml) contains 50mM MES buffer (PH 5.0), 100mM NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
CD38 is a surface molecule which acts as a plasma membrane signaling receptor in leukocytes. Furthermore, CD38 functions as signaling channel which leads to to cellular activation and proliferation. CD38 also plays a role as an ectoenzyme with various functions as well as an inducer of Ca2+ mobilization from cytoplasmic stores. CD38 signals acts as a coreceptor on B cells and modulates B cell receptor.
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Synonyms
P28907, ADP-Ribosyl Cyclase 1, 2-Phospho-Cyclic-ADP-Ribose Transferase, Cyclic ADP-Ribose Hydrolase, 2-Phospho-ADP-Ribosyl Cyclase, NAD(+) Nucleosidase, CD38 Antigen (P45), ADPRC 1, 2-Phospho-ADP-Ribosyl Cyclase/2-Phospho-Cyclic-ADP-Ribose Transferase, Ecto-Nicotinamide Adenine Dinucleotide Glycohydrolase , Cluster Of Differentiation 38, CADPr Hydrolase 1,CD38 Antigen, EC 2.4.99.20, EC 3.2.2.6, ADPRC1, T10.
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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
ADPEFVPRWR QQWSGPGTTK RFPETVLARC VKYTEIHPEM RHVDCQSVWD AFKGAFISKH PCNITEEDYQ PLMKLGTQTV PCNKILLWSR IKDLAHQFTQ VQRDMFTLED TLLGYLADDL TWCGEFNTSK INYQSCPDWR KDCSNNPVSV FWKTVSRRFA EAACDVVHVM LNGSRSKIFD KNSTFGSVEV HNLQPEKVQT LEAWVIHGGR EDSRDLCQDP TIKELESIIS KRNIQFSCKN IYRPDKFLQC VKNPEDSSCT SEIHHHHHH.
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 :
TNFSF8 Human, Sf9Description:
CD30 Ligand Human Recombinant, Sf9
Tumor Necrosis Factor Superfamily Member 8, Tumor Necrosis Factor (Ligand) Superfamily, Member 8, CD153 Antigen, CD30 Ligand, CD30LG, CD30-L, CD30L, Tumor Necrosis Factor (Ligand) Superfamily Member 8, Tumor Necrosis Factor Ligand 3A, CD30 Antigen Ligand, TNLG3A, CD153, Tumor necrosis factor ligand superfamily member 8, TNFSF8, CD30 ligand.
Product # :
CYT-954Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TNFSF8 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 181 amino acids (63-234a.a.) and having a molecular mass of 20.7kDa (Molecular size on SDS-PAGE will appear at approximately 18-40kDa). TNFSF8 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TNFSF8 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
CD30 Ligand (TNFSF8) is a cytokine which is a member of the tumor necrosis factor (TNF) ligand family. The TNFSF8 cytokine is a ligand for TNFRSF8/CD30, which is a cell surface antigen and a marker for Hodgkin lymphoma and related hematologic malignancies. The employment of the TNFSF8 cytokine expressed on B cell surface has an inhibitory role in modulating Ig class switch. TNFSF8 enhances cell proliferation of some lymphoma cell lines, while inducing cell death and reducing cell proliferation of other lymphoma cell lines. The pleiotropic biological activities of the TNFSF8 cytokine on different CD30+ lymphoma cell lines has a pathophysiologic role in Hodgkin's and some non-Hodgkin's lymphomas.
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Synonyms
Tumor Necrosis Factor Superfamily Member 8, Tumor Necrosis Factor (Ligand) Superfamily, Member 8, CD153 Antigen, CD30 Ligand, CD30LG, CD30-L, CD30L, Tumor Necrosis Factor (Ligand) Superfamily Member 8, Tumor Necrosis Factor Ligand 3A, CD30 Antigen Ligand, TNLG3A, CD153, Tumor necrosis factor ligand superfamily member 8, TNFSF8, CD30 ligand.
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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
ADPQRTDSIP NSPDNVPLKG GNCSEDLLCI LKRAPFKKSW AYLQVAKHLN KTKLSWNKDG ILHGVRYQDG NLVIQFPGLY FIICQLQFLV QCPNNSVDLK LELLINKHIK KQALVTVCES GMQTKHVYQN LSQFLLDYLQ VNTTISVNVD TFQYIDTSTF PLENVLSIFL YSNSDHHHHH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL17RB MouseDescription:
Interleukin-17 Receptor Beta Mouse Recombinant
Il17rb, Evi27, IL-17ER, IL-17Rh1, Il17br, IL17RH1, IL-17 receptor B, IL-17RB, Interleukin-17 receptor B.
Product # :
CYT-960Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IL17RB produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 511 amino acids (18-286 a.a.) and having a molecular mass of 57.1kDa (Molecular size on SDS-PAGE will appear at approximately 57-70kDa). IL17RB is expressed with an 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL17RB protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
IL17 is a proinflammatory cytokine produced by activated T cells. IL-17 regulates the activities of NF-kappaB and mitogen-activated protein kinases. Interleukin-17 can stimulate the expression of IL6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO). High levels of IL-17 are associated with several chronic inflammatory diseases including rheumatoid arthritis, psoriasis and multiple sclerosis.
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Synonyms
Il17rb, Evi27, IL-17ER, IL-17Rh1, Il17br, IL17RH1, IL-17 receptor B, IL-17RB, Interleukin-17 receptor B.
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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
ADPREPTIQC GSETGPSPEW MVQHTLTPGD LRDLQVELVK TSVAAEEFSI LMNISWILRA DASIRLLKAT KICVSGKNNM NSYSCVRCNY TEAFQSQTRP SGGKWTFSYV GFPVELSTLY LISAHNIPNA NMNEDSPSLS VNFTSPGCLN HVMKYKKQCT EAGSLWDPDI TACKKNEKMV EVNFTTNPLG NRYTILIQRD TTLGFSRVLE NKLMRTSVAI PVTEESEGAV VQLTPYLHTC GNDCIRREGT VVLCSETSAP IPPDDNRRML GGVEPKSCDK 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.
- View Data Sheet
Name :
IL22RA (Y51A) HumanDescription:
Interleukin-22 Receptor Antagonist (Y51A) Human Recombinant
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
Product # :
CYT-1252Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IL22RA (Y51A) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 147 amino acids and having a molecular mass of 16.7 kDa. IL22RA (Y51A) is purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration chromatography.
(b) Analysis by SDS-PAGE.
Biological Activity
IL22RA (Y51A) Is capable of full inhibition of STAT3 phosphorylation induced by mouse interleukin 22 in HepG cells. Its affinity toward immobilized mIL-22 receptor α1 extracellular domain (mIL-22 Rα1-ECD) or IL-22 binding protein is similar to the non mutated mouse interleukin 22. Human IL-22 antagonist (Y51A) has no agonistic activity in this bioassay.
More Info
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Synonyms
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IL22RA (Y51A) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL22RA (Y51A) 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 IL22RA (Y51A) in sterile 18MΩ-cm 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 Ala-Pro-Ile-Ser-Ser.
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Background
IL-22 is a part of the IL-10 family of regulatory cytokines and produced by a few populations of immune cells at a site of inflammation. Members of this family share partial homology in their amino acid sequences, but varies in their biological functions. IL-22 effects on non-hematopoietic cells. IL-22 responsible for wound healing and takes part in protection against microbs. Produced by T lymphocytes, IL-22 inhibits IL-4 production by Th2 cells, and induces acute phase reactants in the pancreas and liver.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.18 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the DNAman computer analysis program of protein sequences.
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 :
AURKB HumanDescription:
Aurora Kinase B Human Recombinant
Serine/threonine-protein kinase 12, Aurora kinase B, Serine/threonine-protein kinase aurora-B, Aurora- and Ipl1-like midbody-associated protein 1, Aurora/IPL1-related kinase 2, Aurora-related kinase 2, AIM-1, ARK-2, STK-1, AURKB, AIK2, AIM1, ARK2, STK12, AurB, IPL1, STK5, aurkb-sv1, aurkb-sv2.
Product # :
PKA-355Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
AURKB Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 364 amino acids (1-344) and having a molecular mass of 41.4kDa. AURKB is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AURKB solution containing 20mM Tris-HCl buffer (pH8.0), 0.5mM DTT, 20% glycerol, 0.1mM EDTA, 0.1mM EGTA, 0.1M NaCl and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Aurora Kinase B (AURKB) belongs to a family of mitotic serine/threonine kinases. AURKB connects with chromosomes for the period of prophase prior to relocalizing to the spindle at anaphase. AURKB localizes to microtubules near kinetochores, specifically to the specialized microtubules called K-fibers. AURKB controls chromosome segregation through the control of microtubule-kinetochore attachment and cytokinesis. AURKB is required for kinetochore localization of BUB1 and SGOL1. AURKB expression during the G2/M phase transition is firmly coordinated with histone H3 phosphorylation, while overexpression is seen in many kinds of cancers. AURKB phosphorylates 'Ser-10' and 'Ser-28' of histone H3 during mitosis. AURKB is a component of the CPC (chromosomal passenger complex), which is a complex that acts as a key regulator of mitosis.
High level expression of AURKB is seen in the thymus, which is also expressed in the spleen, lung, testis, colon, placenta and fetal liver. AURKB is expressed during S and G2/M phase and expression is up-regulated in cancer cells during M phase. -
Synonyms
Serine/threonine-protein kinase 12, Aurora kinase B, Serine/threonine-protein kinase aurora-B, Aurora- and Ipl1-like midbody-associated protein 1, Aurora/IPL1-related kinase 2, Aurora-related kinase 2, AIM-1, ARK-2, STK-1, AURKB, AIK2, AIM1, ARK2, STK12, AurB, IPL1, STK5, aurkb-sv1, aurkb-sv2.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
AURKB although stable at 4°C for 1 week, should be stored 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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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAQKENSYPW PYGRQTAPSG LSTLPQRVLR KEPVTPSALV LMSRSNVQPT AAPGQKVMEN SSGTPDILTR HFTIDDFEIG RPLGKGKFGN VYLAREKKSH FIVALKVLFK SQIEKEGVEH QLRREIEIQA HLHHPNILRL YNYFYDRRRI YLILEYAPRG ELYKELQKSC TFDEQRTATI MEELADALMY CHGKKVIHRD IKPENLLLGL KGELKIADFG WSVHAPSLRR KTMCGTLDYL PPEMIEGRMH NEKVDLWCIG VLCYELLVGN PPFESASHNE TYRRIVKVDL KFPASVPMGA QDLISKLLRH NPSERLPLAQ VSAHPWVRAN SRRVLPPSAL QSVA.
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 :
BCL2 Human, HisDescription:
B-Cell Lymphoma Protein 2 Alpha Human Recombinant, His Tag
Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.
Product # :
PRO-683Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
BCL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 1-211 and having a molecular mass of 25.4 kDa. The BCL2 is fused to a 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BCL2 protein solution contains 20mM Tris-HCl, pH-8, 2mM DTT and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
BCL2 gene encodes an integral outer mitochondrial membrane protein that blocks the apoptotic death of some cells such as lymphocytes. Constitutive expression of BCL2, such as in the case of translocation of BCL2 to Ig heavy chain locus, is thought to be the cause of follicular lymphoma. Two transcript variants, produced by alternate splicing, differ in their C-terminal ends.
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Synonyms
Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.
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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 MAHAGRTGYD NREIVMKYIH YKLSQRGYEW DAGDVGAAPP GAAPAPGIFS SQPGHTPHPA ASRDPVARTS PLQTPAAPGA AAGPALSPVP PVVHLTLRQA GDDFSRRYRR DFAEMSSQLH LTPFTARGRF ATVVEELFRD GVNWGRIVAF FEFGGVMCVE SVNREMSPLV DNIALWMTEY LNRHLHTWIQ DNGGWDAFVE LYGPSMRPLF 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 :
TNFSF7 HumanDescription:
CD70 Human Recombinant
CD70 Molecule, TNFSF7, CD27L, Tumor Necrosis Factor (Ligand) Superfamily, Member 7, Tumor Necrosis Factor Ligand Superfamily Member 7, CD70 Antigen, CD27 Ligand, CD27LG, CD27-L, Surface Antigen CD70, Ki-24 Antigen, CD70 antigen.
Product # :
CYT-880Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TNFSF7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 178 amino acids (39-193 a.a) and having a molecular mass of 19.5kDa. TNFSF7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TNFSF7 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
-
Introduction
CD70 also known as TNFSF7 is a cytokine which binds to CD27. TNFSF7 takes part in T-cell activation as well as induces the proliferation of costimulated T-cells. Moreover, TNFSF7 enhances the generation of cytolytic T-cells. Among the diseases which are associated with TNFSF7: Include acute myocarditis & Myocarditis.
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Synonyms
CD70 Molecule, TNFSF7, CD27L, Tumor Necrosis Factor (Ligand) Superfamily, Member 7, Tumor Necrosis Factor Ligand Superfamily Member 7, CD70 Antigen, CD27 Ligand, CD27LG, CD27-L, Surface Antigen CD70, Ki-24 Antigen, CD70 antigen.
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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 MGSQRFAQAQ QQLPLESLGW DVAELQLNHT GPQQDPRLYW QGGPALGRSF LHGPELDKGQ LRIHRDGIYM VHIQVTLAIC SSTTASRHHP TTLAVGICSP ASRSISLLRL SFHQGCTIAS QRLTPLARGD TLCTNLTGTL LPSRNTDETF FGVQWVRP.
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 :
ADRM1 AntibodyDescription:
Adhesion Regulating Molecule 1, Mouse Anti Human
Proteasomal ubiquitin receptor ADRM1, 110 kDa cell membrane glycoprotein, Gp110, Adhesion-regulating molecule 1, ARM-1, Proteasome regulatory particle non-ATPase 13, hRpn13, Rpn13 homolog, ADRM1, ARM1, Rpn13.
Product # :
ANT-409Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
-
Introduction
Proteasomal ubiquitin receptor ADRM1 (ADRM1) functions as a proteasomal ubiquitin receptor. ADRM1 is an integral plasma membrane protein which promotes cell adhesion. ADRM1 is assumed to undergo O-linked glycosylation. ADRM1 gene expression is induced by gamma interferon in some cancer cells. ADRM1 employs the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.
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Synonyms
Proteasomal ubiquitin receptor ADRM1, 110 kDa cell membrane glycoprotein, Gp110, Adhesion-regulating molecule 1, ARM-1, Proteasome regulatory particle non-ATPase 13, hRpn13, Rpn13 homolog, ADRM1, ARM1, Rpn13.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human ADRM1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human ADRM1 protein 1-407 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and k light chain.
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Clone
PAT34C2AT.
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Applications
The antibody has been tested by ELISA, Western blot analysis, Flow cytometry 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
ADRM1 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.
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Name :
HBe VLP AntibodyDescription:
Anti Hepatitis B Virus e-Virus Like Particle Mouse
Product # :
ANT-771Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Monoclonal antibody Mab-HBe-VLP is used for gold conjugation to prepare competitive assay to test HBe antibody.
Formulation
Phosphate buffered saline pH 7.4.
More Info
-
Introduction
Hepatitis B virus is the main cause for human liver disease, chronic infection frequently causes liver cancer and cirrhosis. The e antigen is found in the circulation, it is found during the active HBV infection, positive result indicates the risk for contagiousness, and is also used as indicator for the effectiveness of HBV treatment. Positive anti-HBeAg specifies an active stage of acute HBV infection that is in its final stages, the risk for contagiousness is dramatically reduced. HBe VLP Antibody is a monoclonal antibody to the aggregated HBeparticle, used with HBe-VLP antigen to manufacture competitive HBe antibody rapid test or ELISA assay.
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Physical Appearance
sterile filtered clear 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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Applications
ELISA, Lateral flow immunoassay.
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Type
Mouse Anti Human Monoclonal.
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Purification Method
Purified monoclonal IgG by protein A 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 :
SUMO2/3 AntibodyDescription:
Small Ubiquitin-Related Modifier 2/3, Mouse Anti Human
Small ubiquitin-related modifier 2, SUMO-2, Ubiquitin-like protein SMT3B, SMT3 homolog 2, Sentrin-2, HSMT3, SUMO-3, SUMO2, SMT3B, SMT3H2, MGC117191.
Product # :
ANT-016Price :
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
Small Ubiquitin-like Modifiers (SUMOs) are a family of small, related proteins that can be enzymatically attached to a target protein by a post-translational modification process termed sumoylation. Unlike ubiquitination, which targets proteins for degradation, sumoylation participates in a number of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability. All SUMO proteins share the conserved ubiquitin domain and the C-terminal diglycine cleavage/attachment site. Human SUMO2, also known as Sentrin2 and SMT3B is synthesized as a 95 amino acid (aa), 11 kDa propeptide that contains a two aa C-terminal prosegment, and an 18 aa N-terminal protein interacting region (aa 33 -50). Following prosegment cleavage, the C-terminal glycine is enzymatically attached to a lysine on a target protein. Human SUMO2 shares 100% sequence identity to SUMO-2 from mouse. SUMO2 also has very high sequence homology to SUMO3 and SUMO4, 86 % and 85%, respectivel
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Synonyms
Small ubiquitin-related modifier 2, SUMO-2, Ubiquitin-like protein SMT3B, SMT3 homolog 2, Sentrin-2, HSMT3, SUMO-3, SUMO2, SMT3B, SMT3H2, MGC117191.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human SUMO2/3 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human SUMO2 amino acids 1-93 purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and k light chain.
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Clone
PAT10F1AT.
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Applications
SUMO2/3 antibody has been tested by ELISA, Western blot and Immunofluorescence 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 and Immunofluorescence is 1:250 ~ 500.
Recommended starting dilution is 1:250. -
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
SUMO2/3 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 :
LY86 HumanDescription:
Lymphocyte Antigen 86 Human Recombinant
Lymphocyte Antigen 86, MD-1 RP105-Associated, Protein MD-1, Ly-86, MMD-1, dJ80N2.1.
Product # :
PRO-1559Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LY86 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (21-162) and having a molecular mass of 18.1kDa.LY86 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LY86 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
LY86 is vital for effective CD180 cell surface expression and is vastly expressed in B-cells, tonsil and monocytes. LY86 collaborate with TLR4 and CD180 to facilitate the essential immune response to bacterial lipopolysaccharide (LPS) and cytokine production.
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Synonyms
Lymphocyte Antigen 86, MD-1 RP105-Associated, Protein MD-1, Ly-86, MMD-1, dJ80N2.1.
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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 MGSGGGGKAW PTHVVCSDSG LEVLYQSCDP LQDFGFSVEK CSKQLKSNIN IRFGIILRED IKELFLDLAL MSQGSSVLNF SYPICEAALP KFSFCGRRKG EQIYYAGPVN NPEFTIPQGE YQVLLELYTE KRSTVACANA TIMCS
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL 16 Human, HisDescription:
Interleukin-16 Human Recombinant, His Tag
IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.
Product # :
CYT-562Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
Interleukin-16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain (502-631 a.a) containing 150 amino acids and having a molecular mass of 15.5kDa. The IL-16 is fused to a 20 a.a His-Tag at N-Terminus.The IL-16 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL-16 His tag protein (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM PMSF & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
IL-16 is a pleiotropic cytokine that functions as a chemoattractant, a modulator of T cell activation, and an inhibitor of HIV replication. The signaling process of IL-16 is mediated by CD4. The product of this gene undergoes proteolytic processing, which is found to yield two functional proteins. IL-16 functions exclusively attributed to the secreted C-terminal peptide, while the N-terminal product may play a role in cell cycle control. Caspase 3 is reported to be involved in the proteolytic processing of this protein. Two transcript variants encoding different isoforms have been found for this gene.
IL-16 stimulates a migratory response in cd4+ lymphocytes, monocytes, and eosinophils. Also induces t-lymphocyte expression of interleukin 2 receptor, ligand for cd4. -
Synonyms
IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.
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Physical Appearance
Sterile Filtered solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPDLNSSTDS AASASAASDV SVESTAEATV CTVTLEKMSAGLGFSLEGGK GSLHGDKPLT INRIFKGAAS EQSETVQPGD EILQLGGTAM QGLTRFEAWN IIKALPDGPV TIVIRRKSLQ SKETTAAGDS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin Super Antagonist RatDescription:
Leptin Super Antagonist Rat Recombinant
Product # :
CYT-1240Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
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Description
Super Leptin Antagonist Rat Recombinant is a single polypeptide chain containing 146 amino acids. Super Rat Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A super Rat leptin antagonist that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
ProSpec’s super Rat leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Super Rat leptin antagonist also inhibits various leptin effects in several in vitro bioassays.
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Super Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of super Rat leptin antagonist at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization super Rat leptin antagonist can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Super Leptin Antagonist in sterile 0.4% NaHCO3 adjusted to pH 8-9, 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 Ala-Val-Pro-Ile-His.
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Background
Leptin is a hormone which takes part in regulating body weight, metabolism and reproductive function and is encoded by the obese gene. Leptin is expressed predominantly by adipocytes, which fits with the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are expressed mainly in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.
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.