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652 results found for “biglycan”
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Name :
SPP1 HumanDescription:
Osteopontin Human Recombinant
Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1.
Product # :
CYT-635Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Secreted Phosphoprotein-1 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 321 amino acids fragment (17-314) and having a total molecular mass of 36.2 kDa(molecular weight on SDS-PAGE will shift up). The SPP1 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Osteopontin is supplied in 20mM Tris-HCl buffer pH-7.5, 1mM DTT, 2mM EDTA and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Osteopontin is a glycoprotein that was first identified in osteoblasts and is involved in bone remodeling, immune functions in fibroblasts, macrophages, and lymphocytes during inflammation and wound healing. SPP1 binds tightly to hydroxyapatite. SPP1 forms an integral part of the mineralized matrix. SPP1 is vital to cell-matrix interaction.
Secreted Phosphoprotein-1 protects against cardiac ischemia-reperfusion injury via late preconditioning. Expression of both Ostepontin and CD44 in hepatocellular carcinoma is linked with advanced tumor stage and contributes to prognosis information. SPP1 is the most over-expressed gene in intrahepatic cholangiocarcinoma. Secreted Phosphoprotein-1 overexpression is related with interstitial lung diseases. -
Synonyms
Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1.
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Physical Appearance
Sterile Filtered clear 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 RSMIPVKQAD SGSSEEKQLY NKYPDAVATW LNPDPSQKQN LLAPQNAVSS EETNDFKQET LPSKSNESHD HMDDMDDEDD DDHVDSQDSI DSNDSDDVDD TDDSHQSDES HHSDESDELV TDFPTDLPAT EVFTPVVPTV DTYDGRGDSV VYGLRSKSKK FRRPDIQYPD ATDEDITSHM ESEELNGAYK AIPVAQDLNA PSDWDSRGKD SYETSQLDDQ SAETHSHKQS RLYKRKANDE SNEHSDVIDS QELSKVSREF HSHEFHSHED MLVVDPKSKE EDKHLKFRIS HELDSASSEV N.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CCL18 Human, HisDescription:
Macrophage Inflammatory protein-4 (CCL18) Human Recombinant, His-Tag
Small inducible cytokine A18, CCL18, Macrophage inflammatory protein 4, MIP-4, Pulmonary and activation-regulated chemokine, CC chemokine PARC, Alternative macrophage activation-associated CC chemokine 1, AMAC-1, Dendritic cell chemokine 1, DC-CK1, chemokine (C-C motif) ligand 18, CKb7, PARC, AMAC1, DCCK1, SCYA18.
Product # :
CHM-339Price :
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Shipped with Ice Packs
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Description
MIP-4 Human Recombinant fused with a 25 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 93 amino acids (22-89 a.a.) and having a molecular mass of 10.4kDa. The MIP-4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MIP-4 solution (0.25 mg/ml) contains 10mM Sodium Citrate pH3.5 and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Chemokine (C-C motif) ligand 18 (CCL18) is a small cytokine belonging to the CC chemokine family that was previously called PARC (pulmonary and activation-regulated chemokine). CCL18 is approximately 60% identical in amino acid sequence to CCL3. It is expressed at high levels in lung and at lower levels in certain lymphoid tissues, such as the lymph nodes, and is chemotactic for activated T cells and non activated lymphocytes. The gene for human CCL18 contains three exons and is located on chromosome 17.
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Synonyms
Small inducible cytokine A18, CCL18, Macrophage inflammatory protein 4, MIP-4, Pulmonary and activation-regulated chemokine, CC chemokine PARC, Alternative macrophage activation-associated CC chemokine 1, AMAC-1, Dendritic cell chemokine 1, DC-CK1, chemokine (C-C motif) ligand 18, CKb7, PARC, AMAC1, DCCK1, SCYA18.
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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 MGSHMQVGTN KELCCLVYTS WQIPQKFIVD YSETSPQCPK PGVILLTKRG RQICADPNKK WVQKYISDLK LNA.
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Background
What is the molecular weight/Mw of CCL18 HUMAN, HIS Protein?
CCL18 HUMAN, HIS Protein has a total Mw of 10.4kDa.
What is the source or expression system of CCL18 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CCL18 HUMAN, HIS Protein?
CCL18 HUMAN, HIS Protein is > 95% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL18 HUMAN, HIS Protein?
The biological functionality of CCL18 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CCL18 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSHMQVGTN KELCCLVYTS WQIPQKFIVD YSETSPQCPK PGVILLTKRG RQICADPNKK WVQKYISDLK LNA.
What applications can CCL18 HUMAN, HIS Protein be used in?
CCL18 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL18 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL18 HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CCL18 HumanDescription:
Macrophage Inflammatory Protein-4 Human Recombinant (CCL18)
Small inducible cytokine A18, CCL18, Macrophage inflammatory protein 4, MIP-4, Pulmonary and activation-regulated chemokine, CC chemokine PARC, Alternative macrophage activation-associated CC chemokine 1, AMAC-1, Dendritic cell chemokine 1, DC-CK1, chemokine (C-C motif) ligand 18, CKb7, PARC, AMAC1, DCCK1, SCYA18.
Product # :
CHM-322Price :
Quantity :
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Shipped at Room temp
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Description
Macrophage Inflammatory Protein-4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7813 Dalton. The MIP-4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MIP-4 protein is lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 100mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Activity MIP-4 is calculated by the ability to chemoattract Human T lymphocytes at 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.More Info
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Introduction
Chemokine (C-C motif) ligand 18 (CCL18 / MIP-4) is a small cytokine belonging to the CC chemokine family that was previously called PARC (pulmonary and activation-regulated chemokine). MIP-4 is approximately 60% identical in amino acid sequence to CCL3. MIP-4 is expressed at high levels in lung and at lower levels in certain lymphoid tissues, such as the lymph nodes, and is chemotactic for activated T cells and non activated lymphocytes. The gene for human CCL18 contains three exons and is located on chromosome 17.
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Synonyms
Small inducible cytokine A18, CCL18, Macrophage inflammatory protein 4, MIP-4, Pulmonary and activation-regulated chemokine, CC chemokine PARC, Alternative macrophage activation-associated CC chemokine 1, AMAC-1, Dendritic cell chemokine 1, DC-CK1, chemokine (C-C motif) ligand 18, CKb7, PARC, AMAC1, DCCK1, SCYA18.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIP-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIP-4 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 MIP-4 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 of MIP-4 was determined and found to be Ala-Gln-Val-Gly-Thr.
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Background
What is the molecular weight/Mw of CCL18 HUMAN Protein?
CCL18 HUMAN Protein has a total Mw of 7.8kDa.
What is the source or expression system of CCL18 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL18 HUMAN Protein?
CCL18 HUMAN Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL18 HUMAN Protein?
The Activity MIP-4 is calculated by the ability to chemoattract Human T lymphocytes at 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of CCL18 HUMAN Protein?
The sequence of the first five N-terminal amino acids of MIP-4 was determined and found to be Ala-Gln-Val-Gly-Thr.
What applications can CCL18 HUMAN Protein be used in?
CCL18 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL18 HUMAN Protein?
The endotoxin level is minimal, CCL18 HUMAN 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 :
IL 2 Human, YeastDescription:
Interleukin-2 Human Recombinant, Yeast
Interleukin-2, T-cell growth factor (TCGF), Interleukin-2, Lymphokine, IL-2.
Product # :
CYT-797Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-2 Human Recombinant produced in yeast is a single, glycosylated polypeptide chain containing 134 amino acids and having a molecular mass of 14 kDa. The IL-2 is purified by proprietary chromatographic techniques.
Source
Pichia pastoris.
Formulation
The protein was lyophilized from a 0.2µm filtered solution in 20mM sodium phosphate buffer pH 7.0 in absence of any carrier protein.
Purity
Greater than 98% as determined by SDS-PAGE.
Biological Activity
The biological activity is determined by the dose dependent proliferation of mouse CTLL–2 cells. Optimal concentration for individual application should be determined by a dose response assay. ED50 range = 0.08–0.5ng/mlMore Info
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Introduction
IL2 is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli.
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Synonyms
Interleukin-2, T-cell growth factor (TCGF), Interleukin-2, Lymphokine, IL-2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Interleukin-2 should be stored at 4C between 2-7 days and for future use below -18C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Interleukin-2 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
A P T S S S T K K T Q L Q L E H L L L D L Q M I L N G I N N Y K N P K L T R M L T F K F Y M P K K A T E L K H L Q C L E E E L K P L E E V L N L A Q S K N F H L R P R D L I S N I N V I V L E L K G S E T T F M C E Y A D E T A T I V E F L N R W I T F C Q S I I S T L T.
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 :
Leptin qA Ovine, PEGDescription:
Leptin Quadruple Antagonist Pegylated Ovine Recombinant
Product # :
CYT-1246Price :
Quantity :
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Shipped at Room temp
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Description
Leptin Antagonist Quadruple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Ovine Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. The Ovine Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Ovine Leptin Quadruple anatagonist Pegylated runs as a 48 kDa due to enlarged hydrodymanic volume. Leptin Antagonist Quadruple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Ovine Leptin Quadruple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Pegylated Ovine Leptin Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated recombinant Ovine leptin antagonist in vitro activity is 6-8 fold lower than the non-pegylated recombinant super Ovine leptin antagonist but is 15 fold higher as compared to pegylated recombinant super active ovine leptin antagonist.
More Info
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin Antagonist Quadruple Mutant Ovine Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C 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 Leptin Antagonist Quadruple Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Background
Leptin is mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin effects mostly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor can be found on a various cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviours which save energy. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
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 :
Leptin tA RatDescription:
Leptin Antagonist Triple Mutant Rat Recombinant
Product # :
CYT-355Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Antagonist Triple Mutant Rat Recombinant is a singly non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Rat Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (0.85mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
ProSpec’s Leptin Antagonist Triple Mutant Rat Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It 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 Leptin-Antagonist Triple Mutant Rat Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP-tA mutant can be stored at 4°C 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 Leptin Antagonist Triple Mutant Rat Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with 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-Gln.
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Protein content
Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.21 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).
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 :
PSPN HumanDescription:
Persephin Human Recombinant
Persephin, PSP, PSPN.
Product # :
CYT-801Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
PSPN Human Recombinant produced in E.Coli is a disulfide-linked homodimer containing 2x96 amino acids and having a molecular mass of 20.5kDa. The PSPN is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using human TT medullary thyroid cancer cells is less than 10ng/ml, corresponding to a specific activity of > 1.0 × 100,000 IU/mg.More Info
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Introduction
Persephin is a member of the GDNF ligand subfamily of the TGF-beta superfamily. PSPN encourages the existence and growth of key dopaminergic and motor neurons, as well as taking part in kidney development. Nonetheless, persephin does not support existence of peripheral neurons.
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Synonyms
Persephin, PSP, PSPN.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PSPN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PSPN 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 PSPN in 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
ALSGPCQLWS LTLSVAELGL GYASEEKVIF RYCAGSCPRG ARTQHGLALA RLQGQGRAHG GPCCRPTRYT DVAFLDDRHR WQRLPQLSAA ACGCGG.
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 :
FCGR3A Human, HEKDescription:
CD16a Human Recombinant, HEK
Low affinity immunoglobulin gamma Fc region receptor III-A, CD16a antigen, Fc-gamma, RIII-alpha, Fc-gamma RIII, Fc-gamma RIIIa, FcRIII, FcRIIIa, FcR-10, IgG Fc receptor III-2, CD16a, FCGR3A, FCG3, FCGR3, IGFR3, CD16, FCGRIII.
Product # :
PRO-2770Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FCGR3A Human Recombinant produced HEK293 Cells is a single, polypeptide chain containing 197 amino acids (18-208 a.a) and having a molecular mass of 22.6 kDa. FCGR3A is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 Cells
Formulation
FCGR3A protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Determined by the binding ability in a functional ELISA with Human IgG1 Fc (cat# pro-2763).
More Info
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Introduction
Low affinity immunoglobulin gamma Fc region receptor III-A (FCGR3A) is a receptor for the Fc portion of immunoglobulin G, and is involved in the elimination of antigen-antibody complexes from the circulation, as well as other antibody-dependent responses. FCGR3A needs to associate with the gamma subunit of Fc epsilon. The FCGR3A receptor is expressed on natural killer (NK) cells as an integral membrane glycoprotein anchored through a transmembrane peptide, while FCGR3B is expressed on polymorphonuclear neutrophils (PMN) where the receptor is anchored through a phosphatidylinositol (PI) linkage. In addition, FCGR3A is expressed on macrophages, subpopulation of T-cells, immature thymocytes and placental trophoblasts. FCGR3A mediates antibody-dependent cellular cytotoxicity (ADCC) and other antibody-dependent responses, such as phagocytosis. FCGR3A gene mutations are linked with susceptibility to recurrent viral infections, susceptibility to systemic lupus erythematosus, and alloimmune neonatal neutropenia.
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Synonyms
Low affinity immunoglobulin gamma Fc region receptor III-A, CD16a antigen, Fc-gamma, RIII-alpha, Fc-gamma RIII, Fc-gamma RIIIa, FcRIII, FcRIIIa, FcR-10, IgG Fc receptor III-2, CD16a, FCGR3A, FCG3, FCGR3, IGFR3, CD16, FCGRIII.
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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
MRTEDLPKAV VFLEPQWYRV LEKDSVTLKC QGAYSPEDNS TQWFHNESLI SSQASSYFID AATVDDSGEY RCQTNLSTLS DPVQLEVHIG WLLLQAPRWV FKEEDPIHLR CHSWKNTALH KVTYLQNGKG RKYFHHNSDF YIPKATLKDS GSYFCRGLFG SKNVSSETVN ITITQGLAVS TISSFFPPGY Q HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SSX2 HumanDescription:
Synovial Sarcoma, X Breakpoint 2 Human Recombinant
Cancer/testis antigen family 5, member 2b, CT5.2b, Protein SSX2, Cancer/testis antigen 5.2, Synovial sarcoma, X breakpoint 2, CT5.2, Tumor antigen HOM-MEL-40, SSX2, SSX2A, SSX2B.
Product # :
PRO-1996Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SSX2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-188a.a) and having a molecular mass of 24.0kDa. SSX2 is fused to a 22 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SSX2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Synovial Sarcoma, X Breakpoint 2 (SSX2) is a part of the family of highly homologous synovial sarcoma X breakpoint proteins which play a role as transcriptional repressors. Homologous synovial sarcoma X breakpoint proteins are also able to bring out spontaneous humoral and cellular immune responses in cancer patients, and are effective targets in cancer vaccine-based immunotherapy.
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Synonyms
Cancer/testis antigen family 5, member 2b, CT5.2b, Protein SSX2, Cancer/testis antigen 5.2, Synovial sarcoma, X breakpoint 2, CT5.2, Tumor antigen HOM-MEL-40, SSX2, SSX2A, SSX2B.
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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 RSMNGDDAFA RRPTVGAQIP EKIQKAFDDI AKYFSKEEWE KMKASEKIFY VYMKRKYEAM TKLGFKATLP PFMCNKRAED FQGNDLDNDP NRGNQVERPQ MTFGRLQGIS PKIMPKKPAE EGNDSEEVPE ASGPQNDGKE LCPPGKPTTS EKIHERSGPK RGEHAWTHRL RERKQLVIYE EISDPEEDDE.
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 :
TSG HumanDescription:
Twisted Gastrulation Protein Human Recombinant
Twisted Gastrulation BMP Signaling Modulator 1, TSG, Twisted Gastrulation Homolog 1 (Drosophila), Twisted Gastrulation Protein Homolog 1, Twisted Gastrulation Homolog 1, TWSG1.
Product # :
CYT-873Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TWSG1 Human Recombinant (26-223) produced in CHO is a single, glycosylated, polypeptide chain containing 198 amino acids and having a molecular mass ranging from 35-43kDa on SDS-PAGE due to glycosylation.The TWSG1 is purified by proprietary chromatographic techniques.
Source
CHO.
Formulation
Lyophilized from a 0.2µm filtered solution in PBS.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured by its ability to inhibit alkaline phosphatase production induced by rHuBMP-6 in mouse ATDC5 cells, is less than 16µg/ml.More Info
-
Introduction
Twisted gastrulation Protein (TSG) is a secreted, cysteine-rich protein which has a role in dorsal/ventral patterning in Drosophila and Xenopus by regulating BMP signaling. TSG functions as an agonist for BMP signaling by controlling the inhibitory actions of the BMP antagonist, Chordin/Sog, and the cleavage properties of the metalloprotease, xolloid/tolloid. TSG N-terminal domain binds BMP protein directly and displays BMP antagonist activity.
-
Synonyms
Twisted Gastrulation BMP Signaling Modulator 1, TSG, Twisted Gastrulation Homolog 1 (Drosophila), Twisted Gastrulation Protein Homolog 1, Twisted Gastrulation Homolog 1, TWSG1.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized TSG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TSG should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized TSG in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
CNKALCASDV SKCLIQELCQ CRPGEGNCSC CKECMLCLGA LWDECCDCVG MCNPRNYSDT PPTSKSTVEE LHEPIPSLFR ALTEGDTQLN WNIVSFPVAE ELSHHENLVS FLETVNQPHH QNVSVPSNNV HAPYSSDKEH MCTVVYFDDC MSIHQCKISC ESMGASKYRW FHNACCECIG PECIDYGSKT VKCMN CMF.
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 17 HumanDescription:
Interleukin-17 Human Recombinant
CTLA-8, IL-17, IL-17A, Cytotoxic T-lymphocyte-associated antigen 8.
Product # :
CYT-250Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
- purity
- biological activity
- More Info
- sds-page
Description
Interleukin-17A Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated polypeptide chain containing a total of 264 amino acids (2 chains of 132 aa) and having a molecular mass of 31kDa. The IL-17 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Sterile filtered lyophilized (freeze-dried) powder, with 20mM Citrate, 0.1M NaCl, pH4.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependent induction of IL-6 in Hs68 cell line was found to be approximately 2ng/ml corresponding to a Specific Activity of 500,000IU/mg.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.
-
Synonyms
CTLA-8, IL-17, IL-17A, Cytotoxic T-lymphocyte-associated antigen 8.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Interleukin 17A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL17 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Interleukin 17 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.13 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-17 as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CXCL8 Human, PichiaDescription:
Interleukin-8 (1-77 a.a.) Human Recombinant, (CXCL8) Pichia
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
Product # :
CHM-349Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Interleukin-8 Human Recombinant produced in Yeast is a single, glycosylated polypeptide chain containing 79 amino acids and having a molecular mass of 9 kDa. The IL-8 is purified by proprietary chromatographic techniques.
Source
Pichia Pastoris.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM sodium phosphate buffer pH-8.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Biological Activity
Chemotactic activity was reached at 25ng/ml on human neutrophils.
More Info
-
Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies.
When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor. -
Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Interleukin 8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Background
What is the molecular weight/Mw of CXCL8 HUMAN, PICHIA Protein?
CXCL8 HUMAN, PICHIA Protein has a total Mw of 9kDa.
What is the source or expression system of CXCL8 HUMAN, PICHIA Protein?
Pichia Pastoris.
What is the Purity of CXCL8 HUMAN, PICHIA Protein?
CXCL8 HUMAN, PICHIA Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL8 HUMAN, PICHIA Protein?
Chemotactic activity was reached at 25ng/ml on human neutrophils.
What is the amino acid sequence of CXCL8 HUMAN, PICHIA Protein?
CXCL8 HUMAN, PICHIA Protein is composed from 79 amino acids.
What applications can CXCL8 HUMAN, PICHIA Protein be used in?
CXCL8 HUMAN, PICHIA Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL8 HUMAN, PICHIA Protein?
The endotoxin level is minimal, CXCL8 HUMAN, PICHIA Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IFI30 HumanDescription:
IFN Gamma-Inducible protein 30 Human Recombinant
IFI30, Gamma-IFN-Inducible Lysosomal Thiol Reductase, IFN Gamma-Inducible Protein 30 Preproprotein, Gamma-IFN-Inducible Protein IP-30, Legumaturain, GILT, IP30, IFI-30, MGC32056, EC 1.8.
Product # :
CYT-183Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
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- More Info
- SDS-PAGE
Description
IFI30 Human Recombinant produced in E. coli is a single polypeptide chain containing 199 amino acids (58-232) and having a molecular mass of 22.5 kDa. IFI30 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The IFI30 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
SDS-PAGE
More Info
-
Introduction
IFNI30 inducible lysosomal thiol reductase (IFI30), is a part of the GILT family. IFI30 is a lysosomal thiol reductase which at low pH is capable of decreasing protein’s disulfide bonds. IFI30 is expressed constitutively in antigen-presenting cells and induced by gamma-IFN in other cell types. Also, IFI30 plays an important role in MHC class II-restricted antigen processing. IFI30 facilitates the generation of MHC class II-restricted epitopes from disulfide bond-containing antigen by the endocytic reduction of disulfide bonds and Also facilitates MHC class I-restricted recognition of exogenous antigens containing disulfide bonds by CD8+ T-cells or cross-presentation.
-
Synonyms
IFI30, Gamma-IFN-Inducible Lysosomal Thiol Reductase, IFN Gamma-Inducible Protein 30 Preproprotein, Gamma-IFN-Inducible Protein IP-30, Legumaturain, GILT, IP30, IFI-30, MGC32056, EC 1.8.
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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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNAPLVN VTLYYEALCG GCRAFLIREL FPTWLLVMEI LNVTLVPYGN AQEQNVSGRW EFKCQHGEEE CKFNKVEACV LDELDMELAF LTIVCMEEFE DMERSLPLCL QLYAPGLSPD TIMECAMGDR GMQLMHANAQ RTDALQPPHE YVPWVTVNGK PLEDQTQLLT LVCQLYQGK.
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Background
What is the molecular weight/Mw of IFI30 HUMAN Protein?
IFI30 HUMAN Protein has a total Mw of 22.5kDa.
What is the source or expression system of IFI30 HUMAN Protein?
Escherichia Coli.
What is the Purity of IFI30 HUMAN Protein?
IFI30 HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of IFI30 HUMAN Protein?
The biological functionality of IFI30 HUMAN Protein will be determined in the future.
What is the amino acid sequence of IFI30 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSMNAPLVN VTLYYEALCG GCRAFLIREL FPTWLLVMEI LNVTLVPYGN AQEQNVSGRW EFKCQHGEEE CKFNKVEACV LDELDMELAF LTIVCMEEFE DMERSLPLCL QLYAPGLSPD TIMECAMGDR GMQLMHANAQ RTDALQPPHE YVPWVTVNGK PLEDQTQLLT LVCQLYQGK.
What applications can IFI30 HUMAN Protein be used in?
IFI30 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IFI30 HUMAN Protein?
The endotoxin level is minimal, IFI30 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL 16 Human, (130 a.a.)Description:
Interleukin-16 Human Recombinant, (130 a.a.)
IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.
Product # :
CYT-536Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Interleukin-16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids and having a molecular mass of 13.5 kDa. The IL-16 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IL-16 was lyophilized at 1 mg/ml in 10mM NaP, pH-7.5.
Purity
Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis SDS-PAGE.Biological Activity
The ED50 as determined by its ability to chemoattract human CD4+ T lymphocytes using a concentration range of 10-100ng/ml, corresponding to a Specific Activity of 10,000-100,000 units/mg.More Info
-
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.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Interleukin-16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL16 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Interleukin-16 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Pro-Asp-Leu-Asn.
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 18 Human, HisDescription:
Interleukin-18 Human Recombinant, His Tag
Interferon-gamma-inducing factor, IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin, IL18.
Product # :
CYT-663Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Interleukin-18 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 157 amino acids fragment (37-193) having a molecular weight of 20kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The IL-18 His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Interleukin -18 His-Tag protein is supplied in 20mM Tris-HCl pH-8 and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
IL-18 is a proinflammatory cytokine. This cytokine can induce the IFN-gamma production of T cells. The combination of this cytokine and IL12 has been shown to inhibit IL4 dependent IgE and IgG1 production, and enhance IgG2a production of B cells. IL-18 binding protein (IL18BP) can specifically interact with this cytokine, and thus negatively regulate its biological activity.
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Synonyms
Interferon-gamma-inducing factor, IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin, IL18.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
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 :
OSM Human, 209 a.aDescription:
Oncostatin M Human Recombinant (209 a.a.)
OSM, MGC20461, Oncostatin M.
Product # :
CYT-639Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Oncostatin-M (209 a.a.) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 209 amino acids and having a molecular mass of 23.9kDa. The Oncostatin-M (209 a.a.) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Oncostatin-M (209 a.a.) was lyophilized from a concentrated (1mg/ml) solution containing 1x PBS pH-7.4.
Purity
Greater than 97.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of Human TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000 IU/mg.More Info
-
Introduction
Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.
-
Synonyms
OSM, MGC20461, Oncostatin M.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Oncostatin-M (209 a.a.) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin-M (209 a.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.
-
Solubility
It is recommended to reconstitute the lyophilized Oncostatin-M (209 a.a.) in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
AAIGSCSKEYRVLLGQLQKQTDLMQDTSRLLDPYIRIQGLDVPKLREHCRERPG
AFPSEETLRGLGRRGFLQTLNATLGCVLHRLADLEQRLPKAQDLERSGLNIEDL
EKLQMARPNILGLRNNIYCMAQLLDNSDTAEPTKAGRGASQPPTPTPASDAFQ
RKLEGCRFLHGYHRFMHSVGRVFKWGESPNRSRRHSPHQALRKGVRR.
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 :
OSM MouseDescription:
Oncostatin-M Mouse Recombinant
Oncostatin-M, OSM, OncoM.
Product # :
CYT-168Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
OSM Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 181 amino acids and having a molecular mass of 20.4kDa.The OSM is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
OSM protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependent stimulation of the proliferation of NIH-3T3 mouse embryonic fibroblast cells is < 1 ng/ml, corresponding to a specific activity of > 1.0×106 units/mg.More Info
-
Introduction
Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.
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Synonyms
Oncostatin-M, OSM, OncoM.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Oncostatin M although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Oncostatin M in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
NRGCSNSSSQ LLSQLQNQAN LTGNTESLLE PYIRLQNLNT PDLRAACTQH SVAFPSEDTL RQLSKPHFLS TVYTTLDRVL YQLDALRQKF LKTPAFPKLD SARHNILGIR NNVFCMARLL NHSLEIPEPT QTDSGASRST TTPDVFNTKI GSCGFLWGYH RFMGSVGRVF REWDDGSTRS R.
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 33 HumanDescription:
Interleukin-33 Human Recombinant
Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, NFEHEV, DKFZp586H0523, RP11-575C20.2, IL-33.
Product # :
CYT-425Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
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Description
Interleukin33 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids and having a molecular mass of 18,125 Dalton. The IL-33 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from 10mM NaP pH-7.5.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Interleukin 33 (IL-33) is a 32kDa proinflammatory cytokine that may also regulate gene transcription in producer cells. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1 (IL1 receptor-like-1), which is known also as ST2. Binding of IL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces expression of IL-4, IL-5, IL-13 and leads to severe pathological changes in mucosal organs and in vitro, it can be divided to N-terminal fragment of 12kDa and C-terminal fragment of 18kDa by cleavage of caspase-1.
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Synonyms
Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, NFEHEV, DKFZp586H0523, RP11-575C20.2, IL-33.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized IL-33 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL33 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized IL-33 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MSITGISPIT EYLASLSTYN DQSITFALED ESYEIYVEDL KKDEKKDKVL LSYYESQHPS NESGDGVDGK MLMVTLSPTK DFWLHANNKE HSVELHKCEK PLPDQAFFVL HNMHSNCVSF ECKTDPGVFI GVKDNHLALI KVDSSENLCT ENILFKLSET.
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-1 Alpha Rat, His ActiveDescription:
Interleukin-1 alpha Rat Recombinant, His Tag Active
Interleukin-1 alpha, IL-1 alpha.
Product # :
CYT-1100Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IL1A Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids (115-270 a.a) and having a molecular mass of 20.2kDa.IL1A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
IL1A protein solution (1mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
More Info
-
Introduction
IL-1 alpha is produced by activated macrophages.IL-1 alpha stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1A proteins take part in the inflammatory response, being identified as endogenous pyrogens, and stimulate the release of prostaglandin and collagenase from synovial cells.
-
Synonyms
Interleukin-1 alpha, IL-1 alpha.
-
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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSAPHSFQ NNLRYKLIRI VKQEFIMNDS LNQNIYVDMD
RIHLKAASLN DLQLEVKFDM YAYSSGGDDSKYPVTLKVSN TQLFVSAQGE DKPVLLKEIP
ETPKLITGSE TDLIFFWEKI NSKNYFTSAA FPELLIATKE QSQVHLARGL PSMIDFQIS.
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 :
IL36A MouseDescription:
Interleukin-36 Alpha Mouse Recombinant
Interleukin 36 alpha, FIL1E, IL1F6, FIL1, IL1(EPSILON), interleukin 1 family member 6 (epsilon), MGC129552, MGC129553.
Product # :
CYT-162Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- biological activity
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Description
IL36A Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids and having a molecular mass of 21.0kDa.The IL36A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured by its binding ability in a functional ELISA to bind recombinant mouse IL-1 Rrp2.More Info
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Introduction
Murine IL-36a belongs to the IL-1 family that includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36ra (IL1F5), IL-36b (IL1F8), IL-36g (IL1F9), IL-37 (IL1F7) and IL-38 (IL-1F10). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. Murine IL-36a is a 160 amino acid intracellular and secreted protein which holds no signal sequence, no prosegment and no potential N-linked glycosylation sites. IL-36a is released as a reaction to LPS and the cell ATP-induced activation of the P2X7 receptor.
Mouse to human, full length IL-36a/IL-1F6 shares 54% aa sequence homology. IL-36a is mostly found in skin and lymphoid tissues, but also in fetal brain, trachea, stomach and intestine. -
Synonyms
Interleukin 36 alpha, FIL1E, IL1F6, FIL1, IL1(EPSILON), interleukin 1 family member 6 (epsilon), MGC129552, MGC129553.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IL36A Mouse although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL36A 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 IL36A 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
MNKEKELRAA SPSLRHVQDL SSRVWILQNN ILTAVPRKEQ TVPVTITLLP CQYLDTLETN RGDPTYMGVQ RPMSCLFCTK DGEQPVLQLG EGNIMEMYNK KEPVKASLFY HKKSGTTSTF ESAAFPGWFI AVCSKGSCPL ILTQELGEIF ITDFEMIVVH
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 :
IL5 Mouse, HEKDescription:
Interleukin-5 Mouse Recombinant, HEK
interleukin 5, Il, Il-5, B-cell growth factor II, EDF, BCGF-II, Cytotoxic T-lymphocyte inducer, Eosinophil differentiation factor, TRFB cell differentiation factor I, T-cell replacing factor, TRF, B-cell differentiation factor I, IL5
Product # :
CYT-1194Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IL5 Mouse Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 122 amino acids (21-133 a.a) and having a molecular mass of 14.2 kDa.IL5 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The IL5 solution (0.25mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 3 ng/ml.
More Info
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Introduction
The protein encoded by this gene is a cytokine that acts as a growth and differentiation factor for both B cells and eosinophils. IL5is a main regulator of eosinopoiesis, eosinophil maturation and activation. The elevated production of IL5is reported to be related to asthma or hypereosinophilic syndromes. The receptor of IL5is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). IL5, together with those for interleukin 4 (IL4), interleukin 13 (IL13), and CSF2, form a cytokine gene cluster on chromosome 5. IL5, IL4, and IL13 are found to be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31.
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Synonyms
interleukin 5, Il, Il-5, B-cell growth factor II, EDF, BCGF-II, Cytotoxic T-lymphocyte inducer, Eosinophil differentiation factor, TRFB cell differentiation factor I, T-cell replacing factor, TRF, B-cell differentiation factor I, IL5
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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
DGSMEIPMST VVKETLTQLS AHRALLTSNE TMRLPVPTHK NHQLCIGEIF QGLDILKNQT VRGGTVEMLF QNLSLIKKYI DRQKEKCGEE RRRTRQFLDY LQEFLGVMST EWAMEGHHHH HH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
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 :
Quantity :
Shipping Method :
Shipped with Ice Packs
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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
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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.
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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
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 :
CEA HumanDescription:
Carcinoembryonic Antigen Human Recombinant
CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.
Product # :
PRO-287Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CEA Human Recombinant is glycosylated with N-linked sugars and produced using baculovirus vectors in insect cells. CEA is a well-known tumor marker corresponding to the full length human CEA which is approximately 120,000 Dalton.
Source
Baculovirus Insect Cells.
Formulation
The sterile protein solution contains 10mM NaH2PO4, pH 7 and 150mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Carcinoembryonic antigen (CEA) is a glycoprotein present in fetal digestive-tract tissues; it’s involved in cell adhesion. The production of CEA stops before birth. CEA is called tumor marker since its elevated levels are found in the serum from individuals with colorectal, gastric, pancreatic, lung and breast carcinomas and in heavy smokers.
There are also benign conditions that elevate CEA levels such as smoking, infection, inflammatory bowel disease, pancreatitis, cirrhosis of the liver, and some benign tumors (in the equivalent organs which have cancers with elevated CEA). Typically, higher levels of CEA are found in men, smokers, and older individuals.
The presence of CEA assists in screening, in evaluating recurrent or disseminated disease, and in determining the success of surgical removal of malignant tumors.
CEA levels can be used as indicators of treatment success. The normal values range from 0.0 to 2.5 ng/ml of serum (from blood), in non-smokers, a greater amount than that may be suggestive of cancer. Levels above 20 ng/ml before treatment are associated with cancer which has already metastasized. Benign conditions do not usually cause a CEA increase over 10 ng/ml.
The high levels of CEA should return to normal after successful therapy, however if during follow up there’s an elevation in CEA levels it indicates a recurrence of tumor.
Carcinoembryonic antigen family belongs to the immunoglobulin superfamily; it consists of 29 genes, 18 of which are normally expressed. -
Synonyms
CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.
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Physical Appearance
Sterile Filtered colourless solution.
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Stability
CEA should be stored at 2-8°C.Avoid freezing.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Myostatin Human, HisDescription:
Myostatin Human Recombinant, His Tag
GDF-8, MSTN, Growth/Differentiation Factor 8,MSTN Muscle Hypertrophy.
Product # :
CYT-445Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Total 152AA. M.W. 16.7kDa (calculated). N-terminal His-tag and spacer (43AA – highlighted). The AA sequence of the human myostatin part of the fusion protein is corresponding to the UniProtKB/Swiss-Prot entry O14793.
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M acetate buffer, pH 4.5.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Myostatin (GDF-8) is expressed uniquely in human skeletal muscle as a 12 kDa mature glycoprotein consisting of 113 amino acid residues and secreted into plasma. Myostatin is a member of the transforming growth factor ? superfamily of secreted growth and differentiation factors that is essential for proper regulation of skeletal muscle mass. Studies have shown that myostatin could play an important role in cardiac development and physiology.
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Synonyms
GDF-8, MSTN, Growth/Differentiation Factor 8,MSTN Muscle Hypertrophy.
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Physical Appearance
Filtered white lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDPSSRSAVR SRRDFGLDCD EHSTESRCCR YPLTVDFEAFGWDWIIAPKR YKANYCSGEC EFVFLQKYPH THLVHQANPR GSAGPCCTPT KMSPINMLYF NGKEQIIYGKIPAMVVDRCG CS.
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.