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1000 results found for “Septin”
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Name :
PTMS HumanDescription:
Prothymosin Human Recombinant
ParaT, parathymosin.
Product # :
PRO-1735Price :
Quantity :
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Shipped with Ice Packs
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Description
PTMS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 125 amino acids (1-102aa) and having a molecular mass of 13.9kDa.PTMS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PTMS protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Parathymosin, also known as PTMS is a member of the pro/parathymosin family. PTMS may mediate immune function by blocking the effect of prothymosin alpha which confers resistance to particular opportunistic infections. Among the diseases associated with PTMS are hepatitis b, and alzheimer's disease.
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Synonyms
ParaT, parathymosin.
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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 MGSMSEKSVE AAAELSAKDL KEKKEKVEEK ASRKERKKEV VEEEENGAEE EEEETAEDGE EEDEGEEEDE EEEEEDDEGP ALKRAAEEED EADPKRQKTE NGASA
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 :
MAP2K6 Human, sf9Description:
Mitogen-Activated Protein Kinase Kinase 6 Human Recombinant, sf9
Angiopoietin-1 receptor, Endothelial tyrosine kinase, HYK, STK1, Tunica interna endothelial cell kinase, Tyrosine kinase with Ig and EGF homology domains-2, Tyrosine-protein kinase receptor TEK, Tyrosine-protein kinase receptor TIE-2, mTIE2, p140 TEK, CD202b.
Product # :
PKA-079Price :
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Description
MAP2K6 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 340 amino acids (1-334 a.a.) and having a molecular mass of 38.3kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).MAP2K6 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
MAP2K6 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Mitogen-Activated Protein Kinase 6 (MAP2K6) is a part of the dual specificity protein kinase family. MAP2K6 phosphorylates and activates p38 MAP kinase in response to inflammatory cytokines or environmental stress. MAP2K6 is a vital component of the MAP kinase signal transduction pathway. MAP2K6 takes part in various cellular processes such as stress induced cell cycle arrest and apoptosis.
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Synonyms
Angiopoietin-1 receptor, Endothelial tyrosine kinase, HYK, STK1, Tunica interna endothelial cell kinase, Tyrosine kinase with Ig and EGF homology domains-2, Tyrosine-protein kinase receptor TEK, Tyrosine-protein kinase receptor TIE-2, mTIE2, p140 TEK, CD202b.
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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
MSQSKGKKRN PGLKIPKEAF EQPQTSSTPP RDLDSKACIS IGNQNFEVKA DDLEPIMELG RGAYGVVEKM RHVPSGQIMA VKRIRATVNS QEQKRLLMDL DISMRTVDCP FTVTFYGALF REGDVWICME LMDTSLDKFY KQVIDKGQTI PEDILGKIAV SIVKALEHLH SKLSVIHRDV KPSNVLINAL GQVKMCDFGI SGYLVDSVAK TIDAGCKPYM APERINPELN QKGYSVKSDI WSLGITMIEL AILRFPYDSW GTPFQQLKQV VEEPSPQLPA DKFSAEFVDF TSQCLKKNSK ERPTYPELMQ HPFFTLHESK GTDVASFVKL ILGDHHHHHH.
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 :
Bet v 2.0101Description:
Profilin-1 Recombinant
Profilin-1, Allergen Bet v II, Pollen allergen Bet v 2, Bet v 2, BETVII, Bet v 2.0101.
Product # :
PRO-2283Price :
Quantity :
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Description
Recombinant Profilin-1 produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 15,625 Dalton. Bet v 2.0101 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Bet v 2.0101 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Profilin-1 (Bet v 2.0101) binds to actin and affects the structure of the cytoskeleton. At high concentrations, profiling-1 averts the polymerization of actin, whereas it augments it at low concentrations. By binding to PIP2, Profilin-1 inhibits the creation of IP3 and DG.
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Synonyms
Profilin-1, Allergen Bet v II, Pollen allergen Bet v 2, Bet v 2, BETVII, Bet v 2.0101.
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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. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
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 :
Lymphotactin RatDescription:
Lymphotactin (XCL1) Rat Recombinant
XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.
Product # :
CHM-038Price :
Quantity :
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Shipped at Room temp
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Description
Lymphotactin (XCL1) Rat Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of approximately 10.0kDa.Lymphotactin 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 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a chemotaxis bioassay using human XCR1 transfected murine BaF3 cells < 100 ng/ml, corresponding to a specific activity of > 1.0 × 104 IU/mg.
More Info
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Introduction
XCL1 is a small cytokine belongs to the XC chemokine family that is also known as lymphotactin. XCL1 is found in high levels in spleen, thymus, intestine and peripheral blood leukocytes, and at lower levels in lung, prostate gland and ovary. Cellular sources for XCL1 include activated thymic and peripheral blood CD8+ T cells. This chemokine attracts T cells. In humans, XCL1 is closely related to XCL2, whose gene is found at the same locus on chromosome 1. XCL1 induces it chemotactic function by binding to a chemokine receptor called XCR1.
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Synonyms
XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized XCL1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Lymphotactin 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 Lymphotactin 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
VGTEVLQESI CVSLRTQRLP VQKIKTYTIK EGAMRAVIFV TKRGLRICAD PQAKWVKTAI KTVDGRASAS KSKAETIPTQ AQRSASTAVT LTG.
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 :
Streptavidin AntibodyDescription:
Streptavidin, Mouse Antibody
Product # :
ANT-345Price :
Quantity :
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Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, 0.02% Sodium Azide and 10% glycerol.
More Info
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Introduction
Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is wilyde used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.
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Physical Appearance
Sterile Filtered clear solution.
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Immunogen
Anti Streptavidin mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant Streptavidin amino acids 25-183 purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
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Clone
P1C2AT.
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Applications
Streptavidin antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Antibody 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
Streptavidin 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 :
BD14 MouseDescription:
Beta Defensin-14 Mouse Recombinant
Beta-defensin 14, BD-14, mBD-14, Defensin, beta 14, Defb14.
Product # :
CYT-945Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Beta Defensin-14 Mouse Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 45 amino acids and having a molecular mass of 5.2kDa.The BD14 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BD-14 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 96.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Alpha and Beta Defensins are cationic peptides with antimicrobial activity against Gram-negative and Gram-positive bacteria, fungi and enveloped viruses. These 2-6kDa proteins have vital roles in innate immune system. Mammalian Defensins are classified into alpha, beta and theta categories, based on their size and pattern of disulfide bonding. Beta-Defensins contain a six-cysteine motif which forms 3 intra-molecular disulfide bonds. Since beta-defensins are cationic peptides, they can therefore interact with the membrane of invading microbes, which are negative due to lipopolysaccharides (LPS) and lipoteichoic acid (LTA) found in the cell membrane. In addition, they can affect the stability of the membrane.
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Synonyms
Beta-defensin 14, BD-14, mBD-14, Defensin, beta 14, Defb14.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Mouse BD14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-14 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 BD14 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
FLPKTLRKFF CRIRGGRCAV LNCLGKEEQI GRCSNSGRKC CRKKK.
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Background
What is the molecular weight/Mw of BD14 Protein?
BD14 Protein has a total Mw of 5.2kDa.
What is the source or expression system of BD14 Protein?
Escherichia Coli.
What is the Purity of BD14 Protein?
BD14 Protein is >96% pure as determined by SDS-PAGE.
What is the Biological Activity of BD14 Protein?
The biological functionality of BD14 Protein will be determined in the future.
What is the amino acid sequence of BD14 Protein?
FLPKTLRKFF CRIRGGRCAV LNCLGKEEQI GRCSNSGRKC CRKKK.
What applications can BD14 Protein be used in?
BD14 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BD14 Protein?
The endotoxin level is minimal, BD14 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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Description:
Porcine Follicle Stimulating Hormone
Follitropin, Follicle-stimulating hormone, FSH.
Product # :
HOR-285Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
FSH Porcine is a glycoprotein produced from pituitaries of porcine. The FSH is purified by proprietary chromatographic techniques.
Source
Porcine pituitaries.
Formulation
The FSH was lyophilized with no additives.
More Info
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Introduction
Follicle stimulating hormone (FSH) is a hormone synthesised and secreted by gonadotropes in the anterior pituitary gland. FSH and LH act synergistically in reproductionIn women, in the ovary FSH stimulates the growth of immature Graafian follicles to maturation. As the follicle grows it releases inhibin, which shuts off the FSH production.
In men, FSH enhances the production of androgen-binding proteinby the Sertoli cells of the testes and is critical for spermatogenesis.
In both males and females, FSH stimulates the maturation of germ cells. In females, FSH initiates follicular growth, specifically affecting granulosa cells. With the concomitant rise in inhibin B FSH levels then decline in the late follicular phase. This seems to be critical in selecting only the most advanced follicle to proceed to ovulation. At the end of the luteal phase, there is a slight rise in FSH that seems to be of importance to start the next ovulatory cycle.
Like its partner, LH, FSH releas -
Synonyms
Follitropin, Follicle-stimulating hormone, FSH.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized porcine FSH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FSH-porcine 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 porcine FSH in sterile 18M-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Specific Activity
40 Units/1mg.
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 :
DEFB116 HumanDescription:
Beta Defensin 116 Human Recombinant
Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.
Product # :
CYT-713Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DEFB116 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 102 amino acids (24-102 a.a) and having a molecular mass of 11.5kDa.DEFB116 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DEFB116 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Beta Defensin 116, also known as DEFB116 is a member of the beta-defensin family.DEFB116 has antibacterial activity. The innate immune system includes antimicrobial peptides that protect multicellular organisms from a diverse spectrum of microorganisms. In addition, Beta-Defensins contain one important family of mammalian antimicrobial peptides.
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Synonyms
Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.
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Physical Appearance
Sterile Filtered clear solution.
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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 MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.
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Background
Title: Beta Defensin 116 Human Recombinant: An Insight into its Antimicrobial Properties and Therapeutic Applications
Abstract:
Beta defensin 116 (BD116) is a key member of the beta defensin family, known for its potent antimicrobial activity against various pathogens. This research paper provides an in-depth analysis of human recombinant BD116, focusing on its production, characterization, and potential applications in antimicrobial therapy. The paper highlights the significance of BD116 in innate immunity and its role in combating microbial infections. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD116 in various infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD116 and its utility as a research tool and a potential antimicrobial agent.Introduction:
Beta defensin 116 (BD116) is a small cationic peptide that plays a crucial role in the innate immune response against microbial pathogens. Human recombinant BD116, produced through genetic engineering techniques, offers a valuable tool for studying its antimicrobial properties and exploring its therapeutic potential.Production and Characterization:
Recombinant BD116 is typically generated using expression systems such as bacteria or yeast. The protein is then purified and characterized to ensure its structural integrity and antimicrobial activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant BD116.Antimicrobial Properties:
BD116 exhibits broad-spectrum antimicrobial activity against bacteria, fungi, and viruses. It functions by disrupting the microbial cell membrane and interfering with essential cellular processes. Recombinant BD116 serves as a valuable tool for investigating the mechanisms underlying its antimicrobial action and exploring its potential as an antimicrobial agent.Therapeutic Implications:
The emergence of multidrug-resistant pathogens poses a significant challenge in the treatment of infectious diseases. Recombinant BD116 holds promise as an alternative therapeutic option due to its potent antimicrobial properties. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD116 in various infectious diseases, including bacterial skin infections and respiratory tract infections.Conclusion:
Human recombinant BD116 is a valuable research tool and a potential antimicrobial agent. Its production, characterization, and applications in antimicrobial therapy contribute to our understanding of innate immunity and the development of novel therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD116 offer promising prospects for combating multidrug-resistant pathogens and improving outcomes in infectious diseases.What is the molecular weight/Mw of DEFB116 Protein?
DEFB116 Protein has a total Mw of 11.5kDa.
What is the source or expression system of DEFB116 Protein?
Escherichia Coli.
What is the Purity of DEFB116 Protein?
DEFB116 Protein is >80% pure as determined by SDS-PAGE.
What is the Biological Activity of DEFB116 Protein?
The biological functionality of DEFB116 Protein will be determined in the future.
What is the amino acid sequence of DEFB116 Protein?
MGSSHHHHHH SSGLVPRGSH MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.
What applications can DEFB116 Protein be used in?
DEFB116 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for DEFB116 Protein?
The endotoxin level is minimal, DEFB116 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IL17A Human, Sf9Description:
Interleukin 17A Human Recombinant, Sf9
Interleukin 17A, CTLA8, IL17, Interleukin 17 (Cytotoxic T-Lymphocyte-Associated Serine Esterase 8), Cytotoxic T-Lymphocyte-Associated Protein 8, Cytotoxic T-Lymphocyte-Associated Antigen 8, CTLA-8, IL-17A, IL-17, Interleukin-17A.
Product # :
CYT-895Price :
Quantity :
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Shipped with Ice Packs
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Description
IL17A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (24-155 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 138 amino acids and having a molecular mass of 15.9kDa.IL17A shows multiple bands between 13.5-28kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL17A protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 20% glycerol, 1mM EDTA and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range ≤ 7 ng/ml. The activity is determined by the IL-6 ELISA in a using NIH/3T3 mouse embryonic fibroblast cells.
More Info
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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
Interleukin 17A, CTLA8, IL17, Interleukin 17 (Cytotoxic T-Lymphocyte-Associated Serine Esterase 8), Cytotoxic T-Lymphocyte-Associated Protein 8, Cytotoxic T-Lymphocyte-Associated Antigen 8, CTLA-8, IL-17A, IL-17, Interleukin-17A.
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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
GITIPRNPGC PNSEDKNFPR TVMVNLNIHN RNTNTNPKRS SDYYNRSTSP WNLHRNEDPE RYPSVIWEAK CRHLGCINAD GNVDYHMNSV PIQQEILVLR REPPHCPNSF RLEKILVSVG CTCVTPIVHH VAHHHHHH
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 :
GPNMB Human, Sf9Description:
Glycoprotein Nmb Human Recombinant, Sf9
Transmembrane glycoprotein NMB, Transmembrane glycoprotein HGFIN, GPNMB, HGFIN, NMB, Glycoprotein (transmembrane) nmb.
Product # :
PRO-2394Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GPNMB Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 462 amino acids (22-474a.a.) and having a molecular mass of 51.8kDa. GPNMB is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
GPNMB protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Glycoprotein Nmb (GPNMB) is a member of the PMEL/NMB family. GPNMB is a type I transmembrane glycoprotein which exhibits homology to the pMEL17 precursor, a melanocyte-specific protein. GPNMB is expressed in the lowly metastatic human melanoma cell lines and xenografts but has no expression in the highly metastatic cell lines. GPNMB might be involved in growth delay and reduction of metastatic potential. GPNMB is up-regulated in a number of cancer cells, including in glioblastoma multiforme. GPNMB is expressed in many melanoma cells, as well as in tissue macrophages, including liver Kuppfer cells and lung alveolar macrophages, in podocytes and in some cells of the ciliary body of the eye (at protein level). GPNMB is hardly detectable in the healthy brain.
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Synonyms
Transmembrane glycoprotein NMB, Transmembrane glycoprotein HGFIN, GPNMB, HGFIN, NMB, Glycoprotein (transmembrane) nmb.
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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
ADPAKRFHDV LGNERPSAYM REHNQLNGWS SDENDWNEKL YPVWKRGDMR WKNSWKGGRV QAVLTSDSPA LVGSNITFAV NLIFPRCQKE DANGNIVYEK NCRNEAGLSA DPYVYNWTAW SEDSDGENGT GQSHHNVFPD GKPFPHHPGW RRWNFIYVFH TLGQYFQKLG RCSVRVSVNT ANVTLGPQLM EVTVYRRHGR AYVPIAQVKD VYVVTDQIPV FVTMFQKNDR NSSDETFLKD LPIMFDVLIH DPSHFLNYST INYKWSFGDN TGLFVSTNHT VNHTYVLNGT FSLNLTVKAA APGPCPPPPP PPRPSKPTPS LGPAGDNPLE LSRIPDENCQ INRYGHFQAT ITIVEGILEV NIIQMTDVLM PVPWPESSLI DFVVTCQGSI PTEVCTIISD PTCEITQNTV CSPVDVDEMC LLTVRRTFNG SGTYCVNLTL GDDTSLALTS TLISVPHHHH 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 :
HSA, Pichia PastorisDescription:
Human Serum Albumin Recombinant, Pichia
Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
Product # :
PRO-2149Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HSA Human Recombinant produced in Pichia Pastoris is a polypeptide chain containing 585 amino acids and having a molecular mass of 67 kDa.The recombinant Albumin is purified by proprietary chromatographic techniques.
Source
Pichia Pastoris.
Formulation
The Recombinant Albumin having a concentration of 200mg/ml contains 140mM sodium chloride and 0.16mM octanoate.
Purity
Greater than 97% as determined by HPLC.
More Info
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Introduction
Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin. Albumin is a soluble, monomeric protein which comprises about one-half of the blood serum protein. Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. Albumin is a globular unglycosylated serum protein of molecular weight 65,000. The human albumin gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
HSA is widely used to stabilize blood volume generally from donors but the fear of contamination such as HIV & Hepatitis has enticed great interest in the recombinant form which is identical to the natural blood. -
Synonyms
Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.
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Physical Appearance
Yellowish gel like solution.
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Stability
Recombinant Albumin although stable at 15°C for 1 week, should be stored at 4°C for longer periods of time.Please prevent freeze-thaw cycles.
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Applications
Recombinant Albumin can be used as a media culture supplement at concentrations up to 5 grams per liter. Gradual adaptation of cell lines over several passages to a concentration of 0.5gr to 2gr per liter.
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 :
Desmin HumanDescription:
Desmin Human Recombinant
Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.
Product # :
PRO-520Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Desmin Human Recombinant having a calculated molecular mass of 53,539 Dalton, showing a 55kDa band on SDS-page, pI-5.16.
Source
Escherichia Coli.
Formulation
Desmin was lyophilized from a 1mg/ml solution containing 30mM Tris-HCl pH 8, 9.5M urea, 2mM DTT, 2mM EDTA and 10mM methylammonium chloride.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Desmin is a muscle-specific class III intermediate filament. Homopolymers of this protein form a stable intracytoplasmic filamentous network connecting myofibrils to each other and to the plasma membrane. Mutations in this gene are associated with desmin-related myopathy, a familial cardiac and skeletal myopathy (CSM), and with distal myopathies.
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Synonyms
Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized Desmin between 2-8°C, do not freeze. Upon reconstitution Desmin should be stored at -20°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Desmin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Reconstitution to filaments
After Desmin is dissolved in 9.5M urea buffer (see formulation), protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4M urea and then to low salt condition (50mM NaCl, 2mM dithiothreitol, 10mM Tris-HCl, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco's PBS).
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 :
IL17A Mouse, Sf9Description:
Interleukin-17A, Sf9 Mouse Recombinant
IL17A, Ctla-8, Ctla8, IL-17, IL-17A, Il17, Interleukin-17A, Cytotoxic T-lymphocyte-associated antigen 8, CTLA-8.
Product # :
CYT-1154Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
IL17A Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 141 amino acids (26-158 a.a) and having a molecular mass of 16kDa.IL17A is fused to an 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The IL17A solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Interleukin-17A or IL17A is a cytokine, that has a crucial part in chronic & anti-microbial inflammation. Mouse, rat and human share approximately 60% resemblance is the amino acid sequence. IL17A enhances mucosal & epidermal inflammation when an infection from bacteria occurs, it causes production of chemokines, influx of neutrophils & antibacterial proteins production.
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Synonyms
IL17A, Ctla-8, Ctla8, IL-17, IL-17A, Il17, Interleukin-17A, Cytotoxic T-lymphocyte-associated antigen 8, CTLA-8.
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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
AAIIPQSSAC PNTEAKDFLQ NVKVNLKVFN SLGAKVSSRR PSDYLNRSTS PWTLHRNEDP DRYPSVIWEA QCRHQRCVNA EGKLDHHMNS VLIQQEILVL KREPESCPFT FRVEKMLVGV GCTCVASIVR QAALEHHHHH 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 :
FLT1 D7 HumanDescription:
Vascular Endothelial Growth Factor Receptor-1 D1-7 Human Recombinant
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
Product # :
PKA-241Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Soluble FLT1 Human Recombinant fused with the Fc part of human IgG1 produced in baculovirus is disulfide-linked homodimeric, glycosylated, polypeptide containing 751 amino acids and having a molecular mass of 130 kDa. The soluble receptor protein contains only the first 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. The FLT1 fc/Chimera is purified by proprietary chromatographic techniques.
Source
Insect Cells.
Formulation
FLT1 D1-7 was lyophilized from a concentrated (1 mg/ml) sterile solution containing PBS Buffer, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The activity of FLT1/Fc was determined by its ability to inhibit the VEGF-dependent proliferation of human umbilical vein endothelial cells. The ED50 for this effect is typically 10-30 ng/ml, corresponding to a specific activity of 33,333.33-100,000 units/mg.More Info
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Introduction
Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin.
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Synonyms
FLT-1, FLT1, Tyrosine-protein kinase receptor FLT, Flt-1, Tyrosine-protein kinase FRT, Fms-like tyrosine kinase 1, VEGFR-1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized FLT-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution FLT1 should be stored at 4C between 2-7 days and for future use below -18C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized FLT1 Fc/Chimera in PBS not less than 50µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MVSYWDTGVL LCALLSCLLL TGSSSGSKLK DPELSLKGTQ HIMQAGQTLH LQCRGEAAHK WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN HTGFYSCKYL AVPTSKKKET ESAIYIFISD TGRPFVEMYS EIPEIIHMTE GRELVIPCRV TSPNITVTLK KFPLDTLIPD GKRIIWDSRK GFIISNATYK EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV KLLRGHTLVL NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK RSYRLSMKVK AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA GNYTILLSIK QSNVFKNLTA TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ ILTCTAYGIP QPTIKWFWHP CNHNHSEARC DFCSNNEESF ILDADSNMGN RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK VGTVGRNISF YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK KEITIRDQEA PYLLRNLSDH TVAISSSTTL DCHANGVPEP QITWFKNNHK IQQEPGIILG PGSSTLFIER VTEEDEGVYH CKATNQKGSV ESSAYLTVQG TAASDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI S.
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 :
AASDHPPT HumanDescription:
Aminoadipate-Semialdehyde Dehydrogenase-Phosphopantetheinyl Transferase Human Recombinant
L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase, 4'-phosphopantetheinyl transferase, Alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase, AASD-PPT, LYS5 ortholog, AASDHPPT, LYS2, LYS5, CGI-80, DKFZp566E2346.
Product # :
ENZ-008Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
AASDHPPT Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 316 amino acids (14-309 a.a.) and having a molecular mass of 36.4kDa. The AASDHPPT is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AASDHPPT solution (1mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0), 1mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
AASDHPPT is a member of the P-Pant transferase superfamily. AASDHPPT catalyzes the post-translational modification of target proteins by phosphopantetheine and can transfer the 4'-phosphopantetheine moiety from coenzyme A to a serine residue of a broad range of acceptors, such as the acyl carrier domain of FASN (in vitro). AASDHPPT is similar to Saccharomyces cerevisiae LYS5, which is required for the activation of the alpha-aminoadipate dehydrogenase in the biosynthetic pathway of lysine. AASDHPPT is found in the heart, skeletal muscle, placenta, testis, brain, pancreas, liver and kidney. It’s been suggested that defects in the human AASDHPPT gene result in pipecolic acidemia.
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Synonyms
L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase, 4'-phosphopantetheinyl transferase, Alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase, AASD-PPT, LYS5 ortholog, AASDHPPT, LYS2, LYS5, CGI-80, DKFZp566E2346.
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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 MEGVRWAFSC GTWLPSRAEW LLAVRSIQPE EKERIGQFVF ARDAKAAMAG RLMIRKLVAE KLNIPWNHIR LQRTAKGKPV LAKDSSNPYP NFNFNISHQG DYAVLAAEPE LQVGIDIMKT SFPGRGSIPE FFHIMKRKFT NKEWETIRSF KDEWTQLDMF YRNWALKESF IKAIGVGLGF ELQRLEFDLS PLNLDIGQVY KETRLFLDGE EEKEWAFEES KIDEHHFVAV ALRKPDGSRH QDVPSQDDSK PTQRQFTILN FNDLMSSAVP MTPEDPSFWD CFCFTEEIPI RNGTKS.
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 :
SERPIND1 HumanDescription:
Serpin Peptidase Inhibitor, Clade D Member 1 Human Recombinant
Serpin Family D Member 1, Cysteine Proteinase Inhibitor Clade D Member 1, Serpin Peptidase Inhibitor Clade D Member 1, Protease Inhibitor Leuserpin-2, Serpin D1, HCF2, HLS2, Leuserpin 2, D22S673, THPH10, HC-II, HCII, HC2, LS2.
Product # :
PRO-2050Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SERPIND1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 465 amino acids (58-499) and having a molecular mass of 53.3kDa.SERPIND1 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SERPIND1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Serpin Peptidase Inhibitor, Clade D Member 1 (SERPIND1) is a serine proteinase inhibitor which rapidly inhibits thrombin in the presence of dermatan sulfate. SERPIND1 gene is a member of the serpin gene superfamily. SERPIND1 protein contains 5 exons and 4 introns. SERPIND1 shares homology with antithrombin III and other members of the alpha 1-antitrypsin superfamily. SERPIND1 gene mutations are linked with cofactor II deficiency. SERPIND1 protein is activated by dermatan sulfate, and glycosaminoglycans. Allelic variations in the SERPIND1 gene are linked with cofactor II deficiency.
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Synonyms
Serpin Family D Member 1, Cysteine Proteinase Inhibitor Clade D Member 1, Serpin Peptidase Inhibitor Clade D Member 1, Protease Inhibitor Leuserpin-2, Serpin D1, HCF2, HLS2, Leuserpin 2, D22S673, THPH10, HC-II, HCII, HC2, LS2.
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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 MGSDFHKENT VTNDWIPEGE EDDDYLDLEK IFSEDDDYID IVDSLSVSPT DSDVSAGNIL QLFHGKSRIQ RLNILNAKFA FNLYRVLKDQ VNTFDNIFIA PVGISTAMGM ISLGLKGETH EQVHSILHFK DFVNASSKYE ITTIHNLFRK LTHRLFRRNF GYTLRSVNDL YIQKQFPILL DFKTKVREYY FAEAQIADFS DPAFISKTNN HIMKLTKGLI KDALENIDPA TQMMILNCIY FKGSWVNKFP VEMTHNHNFR LNEREVVKVS MMQTKGNFLA ANDQELDCDI LQLEYVGGIS MLIVVPHKMS GMKTLEAQLT PRVVERWQKS MTNRTREVLL PKFKLEKNYN LVESLKLMGI RMLFDKNGNM AGISDQRIAI DLFKHQGTIT VNEEGTQATT VTTVGFMPLS TQVRFTVDRP FLFLIYEHRT SCLLFMGRVA NPSRS.
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 :
STMN1 HumanDescription:
Stathmin-1 Human Recombinant
Metablastin, Phosphoprotein p19, Oncoprotein p18, PP17, PP19, PR22, Prosolin, C1orf215, FLJ32206, MGC138869, MGC138870, STMN1, Stathmin, Leukemia-associated phosphoprotein p18, Op18, Protein Pr22, LAP18, Lag, SMN.
Product # :
PRO-676Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human Stathmin-1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (1-149 a.a) and having a molecular mass of 19.4 kDa. STMN1 is fused to 20 amino acid His Tga at N-Terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The STMN1 protein solution contains 20mM Tris-HCl, pH-8 and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
STMN1 takes part in the regulation of the microtubule filament structure by destabilizing microtubules. STMN1 promotes the disassembly of microtubules and prevents assembly. STMN1 is a ubiquitous cytosolic phosphoprotein which functions as an intracellular relay integrating regulatory signals of the cellular environment. Stathmin functions as an Oncoprotein in regulation of the cell cycle. Stathmin mutation results in uncontrolled cell proliferation. Stathmin expression associates with cervical carcinogenesis and tumor progression, thus Stathmin is an important prognostic marker in cervical carcinoma. STMN1, takes part in the prevenative progression of ER-positive primary in breast cancer. Somatic mutation in STMN1 effects cell homeostasis that leads to tumorigenicity.
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Synonyms
Metablastin, Phosphoprotein p19, Oncoprotein p18, PP17, PP19, PR22, Prosolin, C1orf215, FLJ32206, MGC138869, MGC138870, STMN1, Stathmin, Leukemia-associated phosphoprotein p18, Op18, Protein Pr22, LAP18, Lag, SMN.
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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 MASSDIQVKE LEKRASGQAF ELILSPRSKE SVPEFPLSPP KKKDLSLEEI QKKLEAAEER RKSHEAEVLK QLAEKREHEK EVLQKAIEEN NNFSKMAEEK LTHKMEANKE NREAQMAAKL ERLREKDKHI EEVRKNKESK DPADETEAD.
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 :
STXBP6 HumanDescription:
Syntaxin Binding Protein 6 Human Recombinant
Syntaxin-binding protein 6, Amisyn, STXBP6, HSPC156, Syntaxin Binding Protein 6.
Product # :
PRO-2056Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
STXBP6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a.) and having a molecular mass of 25.9kDa.STXBP6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
STXBP6 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Syntaxin-binding protein 6 (STXBP6) binds components of the SNARE complex and takes part in regulating SNARE complex configuration. STXBP6 forms non-fusogenic complexes with SNAP25 and STX1A and modulates the formation of SNARE complexes and exocytosis.
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Synonyms
Syntaxin-binding protein 6, Amisyn, STXBP6, HSPC156, Syntaxin Binding Protein 6.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSAKSAI SKEIFAPLDE RMLGAVQVKR RTKKKIPFLA TGGQGEYLTY ICLSVTNKKP TQASITKVKQ FEGSTSFVRR SQWMLEQLRQ VNGIDPNGDS AEFDLLFENA FDQWVASTAS EKCTFFQILH HTCQRYLTDR KPEFINCQSK IMGGNSILHS AADSVTSAVQ KASQALNERG ERLGRAEEKT EDLKNSAQQF AETAHKLAMK HKC.
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 :
CASQ2 HumanDescription:
Calsequestrin-2 Human Recombinant
PDIB2, CASQ2, Calsequestrin-2, Calsequestrin cardiac muscle isoform, FLJ26321, FLJ93514.
Product # :
PRO-799Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CASQ2 Human Recombinant fused to 37 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 417 amino acids (20-399 a.a.) and having a molecular mass of 48.4 kDa. The CASQ2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CASQ2 solution contains 20mM Tris-HCl pH-8, 0.1M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
CASQ2 belongs to the calsequestrin family and is localized to the sarcoplasmic reticulum in cardiac and slow skeletal muscle cells. CASQ2 is a calcium binding protein that stores calcium for muscle function. The discharge of calcium bound to CASQ2 through a calcium release channel activates muscle contraction. CASQ2 binds 40 to 50 moles of calcium. CASQ2 mutations result in stress-induced polymorphic ventricular tachycardia, also called catecholaminergic polymorphic ventricular tachycardia 2 which is known fir its bidirectional ventricular tachycardia that causes cardiac arrest.
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Synonyms
PDIB2, CASQ2, Calsequestrin-2, Calsequestrin cardiac muscle isoform, FLJ26321, FLJ93514.
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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).Please avoid freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMEEG LNFPTYDGKD RVVSLSEKNF KQVLKKYDLL CLYYHEPVSS DKVTQKQFQL KEIVLELVAQ VLEHKAIGFV MVDAKKEAKL AKKLGFDEEG SLYILKGDRT IEFDGEFAAD VLVEFLLDLI EDPVEIISSK LEVQAFERIE DYIKLIGFFK SEDSEYYKAF EEAAEHFQPY IKFFATFDKG VAKKLSLKMN EVDFYEPFMD EPIAIPNKPY TEEELVEFVK EHQRPTLRRL RPEEMFETWE DDLNGIHIVA FAEKSDPDGY EFLEILKQVA RDNTDNPDLS ILWIDPDDFP LLVAYWEKTF KIDLFRPQIG VVNVTDADSV WMEIPDDDDL PTAEELEDWI EDVLSGKINT EDDDEDDDDD DNSDEEDNDD SDDDDDE.
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 :
KLK7 HumanDescription:
Kallikrein-7 Human Recombinant
kallikrein-related peptidase 7, SCCE, hSCCE, EC 3.4.21.117, hK7, Kallikrein-7, PRSS6, KLK7.
Product # :
ENZ-510Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KLK7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 249 amino acids (30-253) and having a molecular mass of 27.1 kDa.The KLK7 is fused to a 25 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
KLK7 protein 1mg/ml is supplied in 20mM Tris-HCl, pH-8, 2M Urea and 10% Glycerol.
Purity
Greater than 90.0% as determined by Analysis by SDS-PAGE.
More Info
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Introduction
KLK7 catalyzes the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. KLK7 is involved in the activation of precursors to inflammatory cytokines.
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Synonyms
kallikrein-related peptidase 7, SCCE, hSCCE, EC 3.4.21.117, hK7, Kallikrein-7, PRSS6, KLK7.
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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 MGSHMIIDGA PCARGSHPWQ VALLSGNQLH CGGVLVNERW VLTAAHCKMN EYTVHLGSDT LGDRRAQRIK ASKSFRHPGY STQTHVNDLM LVKLNSQARL SSMVKKVRLP SRCEPPGTTC TVSGWGTTTS PDVTFPSDLM CVDVKLISPQ DCTKVYKDLL ENSMLCAGIP DSKKNACNGD SGGPLVCRGT LQGLVSWGTF PCGQPNDPGV YTQVCKFTKW INDTMKKHR.
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 :
GP9 HumanDescription:
Glycoprotein-9 Human Recombinant
Platelet glycoprotein IX, GP-IX, GPIX, Glycoprotein 9, CD42a, Glycoprotein IX (Platelet).
Product # :
PRO-055Price :
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Description
GP9 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 154 amino acids (17-147) and having a molecular mass of 16.8kDa. GP9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GP9 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2M UREA and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Glycoprotein-9 (GP9) is a small membrane glycoprotein found on the surface of human platelets. GP9 forms a one to one noncovalent complex with glycoprotein Ib, a platelet surface membrane glycoprotein complex which functions as a receptor for von Willebrand factor. The complete receptor complex includes noncovalent association of the alpha and beta subunits with the protein and platelet glycoprotein V. GP9 gene defects cause the Bernard-Soulier syndrome, aka giant platelet disease whose patients have unusually large platelets and have a clinical bleeding tendency.
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Synonyms
Platelet glycoprotein IX, GP-IX, GPIX, Glycoprotein 9, CD42a, Glycoprotein IX (Platelet).
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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 MGSTKDCPSP CTCRALETMG LWVDCRGHGL TALPALPART RHLLLANNSL QSVPPGAFDH LPQLQTLDVT QNPWHCDCSL TYLRLWLEDR TPEALLQVRC ASPSLAAHGP LGRLTGYQLG SCGWQLQASW VRPG.
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 :
VCPKMT HumanDescription:
Valosin Containing Protein Lysine Methyltransferase Human Recombinant
Valosin Containing Protein Lysine (K) Methyltransferase, Methyltransferase-Like Protein 21D, VCP Lysine Methyltransferase, Protein-Lysine Methyltransferase METTL21D, Chromosome 14 Open Reading Frame 138, C14orf138, METTL21D, VCP-KMT, EC 2.1.1.- .
Product # :
PRO-2145Price :
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Shipped with Ice Packs
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Description
VCPKMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (1-229 a.a.) and having a molecular mass of 28.2kDa.VCPKMT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
VCPKMT protein solution (1mg/ml) containing 20mM Phosphate buffer saline (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
VCPKMT is a member of the methyltransferase superfamily. VCPKMT is a protein-lysine N-methyltransferase which specifically trimethylates 'Lys-315' of VCP/p97; this alteration reduces VCP ATPase activity.
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Synonyms
Valosin Containing Protein Lysine (K) Methyltransferase, Methyltransferase-Like Protein 21D, VCP Lysine Methyltransferase, Protein-Lysine Methyltransferase METTL21D, Chromosome 14 Open Reading Frame 138, C14orf138, METTL21D, VCP-KMT, EC 2.1.1.- .
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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 MGSMADTLES SLEDPLRSFV RVLEKRDGTV LRLQQYSSGG VGCVVWDAAI VLSKYLETPE FSGDGAHALS RRSVLELGSG TGAVGLMAAT LGADVVVTDL EELQDLLKMN INMNKHLVTG SVQAKVLKWG EEIEGFPSPP DFILMADCIY YEESLEPLLK TLKDISGFET CIICCYEQRT MGKNPEIEKK YFELLQLDFD FEKIPLEKHD EEYRSEDIHI IYIRKKKSKF PS
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 :
IL12 Mouse, Sf9Description:
Interleukin 12, Sf9 Human Recombinant
Interleukin 12 (subunit beta/alpha), IL12b/IL12a, Il-12b/Il-12a, IL-12p40/Il-12p35, Il12p40/Il12p35, p40/p35, Sf9.
Product # :
CYT-1058Price :
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Description
IL12 Mouse Recombinant produced in a baculovirus expression system is a glycosylated disulfide linked (through cysteines in bold) heterodimer comprised of IL12A (23-335aa, total of 319 aa, MW 35.7kDa) and IL12B (23-215aa, total of 199 aa, MW 22.5kDa), having a total predicted molecular mass of 58.3kDa (Molecular weight on SDS-PAGE will appear higher). IL12A is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL12 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
The activity is determined by the IFN-g ELISA in a using NK-92 human natural killer cells. The ED50 for this effect is less or equal to 10ng/ml.
More Info
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Introduction
interleukin 12 subunit beta/alpha or IL12b/IL12a is a growth factor cytokine which increases the lytic activity of NK/lymphokine-activated killer cells, activated T and NK cells and prompt IFN-gamma production (through resting PBMC). IL12b/IL12a is a crucial part to the process of cellular-immunity and activates the differentiation of Th1 cells originates from the precursor T helper cells. The protein is linked to IL23A and creates the IL-23 interleukin, by that, the autoimmune inflammation is induced and autoimmune inflammatory diseases and tumorigenesis are being affected.
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Synonyms
Interleukin 12 (subunit beta/alpha), IL12b/IL12a, Il-12b/Il-12a, IL-12p40/Il-12p35, Il12p40/Il12p35, p40/p35, Sf9.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
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Amino Acid Sequence
IL12B(p40)
MWELEKDVYV VEVDWTPDAP GETVNLTCDT PEEDDITWTS DQRHGVIGSG KTLTITVKEF LDAGQYTCHK GGETLSHSHL LLHKKENGIW STEILKNFKN KTFLKCEAPN YSGRFTCSWL VQRNMDLKFN IKSSSSSPDS RAVTCGMASL SAEKVTLDQR DYEKYSVSCQ EDVTCPTAEE
TLPIELALEA RQQNKYENYS TSFFIRDIIK PDPPKNLQMK PLKNSQVEVS WEYPDSWSTP HSYFSLKFFV RIQRKKEKMK ETEEGCNQKG AFLVEKTSTE VQCKGGNVCV QAQDRYYNSS CSKWACVPCR VRS
IL12A(p35)
RVIPVSGPAR CLSQSRNLLK TTDDMVKTAR EKLKHYSCTA EDIDHEDITR DQTSTLKTCL PLELHKNESC LATRETSSTT RGSCLPPQKT SLMMTLCLGS IYEDLKMYQT EFQAINAALQ NHNHQQIILD KGMLVAIDEL MQSLNHNGET LRQKPPVGEA DPYRVKMKLC ILLHAFSTRV
VTINRVMGYL SSAHHHHHH.
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 :
IL6 Human, Sf9Description:
Interleukin-6 Human Recombinant, Sf9
BSF2, HGF, HSF, IFNB2, IL-6.
Product # :
CYT-1150Price :
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Description
IL6 Human Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 189 amino acids (30-212aa) and having a molecular mass of 21.6kDa.(Migrates at 18-28kDa on SDS-PAGE under reducing conditions).IL6 is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
IL6 protein (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, determined by cell proliferation assay using TF-1 human erythroleukemic cell, is 0.2 - 0.8 ng/ml .
More Info
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Introduction
Interleukin-6 or Il-6 is a cytokine with a large assortment of biological functions. IL-6 it has a crucial part in the last differentiation of b-cells into ig-secreting cells. This cytokine also induces myeloma and plasmacytoma growth. Interleukin-6 induces nerve cells differentiation, among hepatocytes it induces acute phase reactants.
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Synonyms
BSF2, HGF, HSF, IFNB2, IL-6.
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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
VPPGEDSKDV AAPHRQPLTS SERIDKQIRY ILDGISALRK ETCNKSNMCE SSKEALAENN
LNLPKMAEKD GCFQSGFNEE TCLVKIITGL LEFEVYLEYL QNRFESSEEQ ARAVQMSTKV
LIQFLQKKAK NLDAITTPDP TTNASLLTKL QAQNQWLQDM TTHLILRSFK EFLQSSLRAL RQMHHHHHH. -
Background
Production and Applications of Human Recombinant Interleukin-6 in Sf9 Cells
Abstract:
Interleukin-6 (IL-6) holds a central role in immune regulation, inflammation, and hematopoiesis. The production of Human Recombinant IL-6 using the Sf9 insect cell system presents a versatile approach for investigating its biological functions and potential therapeutic applications. This paper outlines the methodology of producing Human Recombinant IL-6 in Sf9 cells and explores its significance in immunological research and clinical studies.
Introduction:
IL-6 is a multifunctional cytokine pivotal in various physiological processes, making it a target of intensive research. The expression of Human Recombinant IL-6 facilitates investigations into its intricate mechanisms and offers potential avenues for therapeutic development. The Sf9 cell system, harnessed from Spodoptera frugiperda, enables efficient recombinant protein expression through baculovirus vectors.
Methods:
Production of Human Recombinant IL-6 involves cloning the human IL-6 gene into a baculovirus transfer vector, which is co-transfected with linearized baculovirus DNA into Sf9 cells. The resultant recombinant baculovirus generates and secretes IL-6 into the culture medium. Purification methods, such as chromatography, ensure the protein's quality and functionality.
Applications:
Human Recombinant IL-6 from Sf9 cells has broad applications. It serves as a critical tool for investigating IL-6's roles in immune responses, inflammation, and hematopoiesis. Additionally, it plays a crucial role in the development of therapies targeting IL-6-associated disorders like autoimmune diseases, chronic inflammatory conditions, and cancer.
Sf9 Expression Advantages:
The Sf9 system offers notable advantages, including post-translational modifications and protein folding, necessary for IL-6's biological activity. Sf9 cells provide a platform for generating properly folded and functional recombinant IL-6, reflecting its native structure and function.
Challenges and Future Prospects:
While Sf9-based expression of Human Recombinant IL-6 offers significant advantages, optimization of expression conditions and scale-up strategies remain challenges. Furthermore, the therapeutic potential of Human Recombinant IL-6 requires in-depth preclinical and clinical investigations.
Conclusion:
The production of Human Recombinant IL-6 in Sf9 cells through baculovirus expression offers a powerful tool to comprehend IL-6's multifaceted roles in health and disease. This technology is poised to expand our knowledge of IL-6-related conditions and catalyze the development of precision therapeutic interventions.
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.