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Description:
TRAIL/APO 2 Ligand (114-281 a.a.) Human Recombinant, Active
Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.
Product # :
CYT-1014Price :
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Shipping Method :
Shipped with Ice Packs
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Description
Soluble TNF-related apoptosis-inducing ligand Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (114-281) and having a molecular mass of 19.6 kDa. The sTRAIL is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TRAIL protein solution (1mg/ml) containing 20mM Tris-HCl pH-7.5, 300mM NaCl, 0.1mM DTT & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Measured in a cell cytotoxicity assay using Jurkat human T lymphocyte. The ED50 for this effect is less or equal to 1 ng/ml.
More Info
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Introduction
TNF-related apoptosis-inducing ligand (TRAIL) is a ligand molecule which induces apoptosis. It is a type II transmembrane protein with homology to other members of the tumor necrosis factor family.
In humans, the gene that encodes for TRAIL is located at chromosome 3q26.
TRAIL binds to the death receptors, DR4 and DR5. The process of apoptosis is caspase-8-dependent. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues. -
Synonyms
Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.
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Physical Appearance
Sterile Filtered colorless liquid.
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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
MVRERGPQRV AAHITGTRGR SNTLSSPNSK NEKALGRKIN SWESSRSGHS FLSNLHLRNGELVIHEKGFY YIYSQTYFRF QEEIKENTKN DKQMVQYIYK YTSYPDPILL MKSARNSCWSKDAEYGLYSI YQGGIFELKE NDRIFVSVTN EHLIDMDHEA SFFGAFLVG.
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 :
LGALS1 HumanDescription:
Galectin-1 Human Recombinant
Galectin-1, GAL1, GAL-1, Lectin galactoside-binding soluble 1, Beta-galactoside- binding lectin L-14-I, Lactose-binding lectin 1, S-Lac lectin 1, Galaptin, 14 kDa lectin, HPL, HBL, Putative MAPK-activating protein PM12, GBP, DKFZp686E23103.
Product # :
CYT-544Price :
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Shipped at Room temp
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Description
LGALS1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 135 amino acids and having a molecular mass of 14.7kDa.The LGALS1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Galectin-1 protein was lyophilized from a concentrated (1mg/ml) containing 10mM sodium phosphate, pH-7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The activity of Human Galectin-1 which is determined by the ability to induce chemotaxis of human THP-1 cells is detectable starting at 100ng/ml, corresponding to a specific activity of 1.0x104 units/mg.More Info
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Introduction
The galectins are a family of beta-galactoside-binding proteins implicated in modulating cell-cell and cell-matrix interactions. Galectin-1 is an autocrine negative growth factor that regulates cell proliferation. Galectin-1 regulates cell apoptosis and cell differentiation. Galectin-1 binds CD45, CD3 and CD4 & inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of lyn kinase. Galectin-1 and its ligands are one of the master regulators of immune responses as T-cell homeostasis and survival, T-cell immune disorders, inflammation and allergies as well as host–pathogen interactions. Galectin-1 expression or overexpression in tumors and/or the tissue surrounding them must be considered as a sign of the malignant tumor progression that is often related to the long-range dissemination of tumoral cells (metastasis), to their dissemination into the surrounding normal tissue, and to tumor immune-escape. Galectin-1 in its oxidized form plays a number of important roles in the regeneration of the central nervous system after injury. The targeted overexpression (or delivery) of Galectin-1 should be considered as a method of choice for the treatment of some kinds of inflammation-related diseases, neurodegenerative pathologies and muscular dystrophies. In contrast, the targeted inhibition of Galectin-1 expression is what should be developed for therapeutic applications against cancer progression. Galectin-1 is thus a promising molecular target for the development of new and original therapeutic tools. There is 88% homology between the human and mouse galectin-1.
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Synonyms
Galectin-1, GAL1, GAL-1, Lectin galactoside-binding soluble 1, Beta-galactoside- binding lectin L-14-I, Lactose-binding lectin 1, S-Lac lectin 1, Galaptin, 14 kDa lectin, HPL, HBL, Putative MAPK-activating protein PM12, GBP, DKFZp686E23103.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Galectin-1 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Galectin-1 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 LGALS1 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
MACGLVASNL NLKPGECLRV RGEVAPDAKS FVLNLGKDSN NLCLHFNPRF NAHGDANTIV CNSKDGGAWG TEQREAVFPF QPGSVAEVCI TFDQANLTVK LPDGYEFKFP NRLNLEAINY MAADGDFKIK CVAFD.
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Background
What is the molecular weight/Mw of LGALS1 HUMAN Protein?
LGALS1 HUMAN Protein has a total Mw of 14.7kDa.
What is the source or expression system of LGALS1 HUMAN Protein?
Escherichia Coli.
What is the Purity of LGALS1 HUMAN Protein?
LGALS1 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS1 HUMAN Protein?
The activity of Human Galectin-1 which is determined by the ability to induce chemotaxis of human THP-1 cells is detectable starting at 100ng/ml, corresponding to a specific activity of 1.0x104 units/mg.
What is the amino acid sequence of LGALS1 HUMAN Protein?
MACGLVASNL NLKPGECLRV RGEVAPDAKS FVLNLGKDSN NLCLHFNPRF NAHGDANTIV CNSKDGGAWG TEQREAVFPF QPGSVAEVCI TFDQANLTVK LPDGYEFKFP NRLNLEAINY MAADGDFKIK CVAFD.
What applications can LGALS1 HUMAN Protein be used in?
LGALS1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS1 HUMAN Protein?
The endotoxin level is minimal, LGALS1 HUMAN Protein was purified using conventional chromatography techniques.
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Protein content
UV spectroscopy at 280 nm using the absorbency value of 0.59 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).
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 :
GST antibodyDescription:
Glutathione-S-transferase, Mouse antibody
Product # :
ANT-164Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Formulation
Lyophilized with no salts.
More Info
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Introduction
GST family of enzymescomprises a long list of cytosolic, mitochondrial, and microsomalproteinsthat are 45-55 kDa (dimer form) size and are capable of multiple reactions with a multitude of substrates, both endogenousand xenobiotic. GST catalyses the conjugation of reduced glutathione meaning the sulfhydryl group, to electrophilic centers on a wide variety of substrates. This activity is useful in the detoxification of endogenous compounds such as peroxidised lipids, as well as the metabolism of xenobiotics. GST binds toxins and function as transport protein. Glutathione S-transferase is used to create the so-called 'GST gene fusion system'. The GST is used to purify and detect proteins of interest. In a GST gene fusion system, the GST sequence is incorporated into an expression vector alongside the gene sequence encoding the protein of interest. Induction of protein expression from the vector's multiple cloning sites results in expression of a fusion protein - the protein of interest fused to the GST protein. This GST-fusion protein can then be purified from cells via its high affinity for glutathione. Fusion proteins offer an important biological assay for direct protein-to-protein interactions. The GST tag has the size of 220 amino acids, which, compared to other tags like the myc- or the FLAG-tag, is quite big. It is fused to the N-terminusof a protein. However, many commercially-available sources of GST-tagged plasmids include a thrombindomain for cleavage of the GST tag during protein purification. A GST-tag is often used to separate and purify proteins that contain the GST-fusion. GST-fusion proteins can be produced in Escherichia coli, as recombinant proteins.
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Solubility
Reconstitute with 1.0 ml of PBS. Mix gently, wash the sides of the vial and wait 30-60 seconds before use. Protein after reconstitution is 2 mgs/ml.
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Immunogen
glutathione-S-transferase (GST) of Schistosoma japonicum.
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Ig Subclass
Mouse IgG1.
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Clone
6C7.
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Specificity
glutathione-S-transferase (GST) of Schistosoma japonicum.
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Type
Mouse Antibody Monoclonal.
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Purification Method
Protein A column.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ACOT11 AntibodyDescription:
Acyl-Coenzyme A Thioesterase 11, Mouse Anti Human
Acyl-coenzyme A thioesterase 11, Acyl-CoA thioesterase 11, Acyl-CoA thioester hydrolase 11, Brown fat-inducible thioesterase, BFIT, Adipose-associated thioesterase, ACOT11, BFIT, KIAA0707, THEA, BFIT1, BFIT2, THEM1, STARD14.
Product # :
ANT-424Price :
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Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, 0.02% Sodium Azide & 10% Glycerol.
More Info
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Introduction
ACOT11 is a protein with acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates. Expression of a similar murine protein in brown adipose tissue is induced by cold exposure and repressed by warmth. Expression of the mouse ACOT11 has been linked to obesity, with higher expression found in obesity-resistant mice compared with obesity-prone mice.
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Synonyms
Acyl-coenzyme A thioesterase 11, Acyl-CoA thioesterase 11, Acyl-CoA thioester hydrolase 11, Brown fat-inducible thioesterase, BFIT, Adipose-associated thioesterase, ACOT11, BFIT, KIAA0707, THEA, BFIT1, BFIT2, THEM1, STARD14.
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Immunogen
Anti-human ACOT11 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human ACOT11 amino acids 19-250 purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and κ light chain.
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Clone
PJ4B2AT.
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Applications
ACOT11 antibody has been tested by ELISA, Western blot and immunohistochemistry analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot is 1:500 ~ 1:2,000 and immunohistochemistry analysis is 1:50~100. Recommended starting dilution for Western blot is 1:1,000 and Immunohistochemistry is 1:100.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
ACOT11 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 :
CKMT1A AntibodyDescription:
Creatine Kinase, Mitochondrial 1A, Mouse Anti Human
Creatine kinase mitochondrial 1A, creatine kinase mitochondrial 1 (ubiquitous), creatine kinase U-type mitochondrial, Acidic-type mitochondrial creatine kinase, Ubiquitous mitochondrial creatine kinase, CKMT1, U-MtCK, mia-CK, EC 2.7.3, EC 2.7.3.2.
Product # :
ANT-519Price :
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Shipping Method :
Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
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Introduction
CKMT1A is in charge of the transfer of high energy phosphate from mitochondria to the cytosolic carrier, creatine. CKMT1A is a member of the creatine kinase isoenzyme family and exists as two isoenzymes, sarcomeric MtCK and ubiquitous MtCK, encoded by separate genes. Mitochondrial creatine kinase arises in two different oligomeric forms: dimers and octamers, unlike the exclusively dimeric cytosolic creatine kinase isoenzymes. Numerous malignant cancers with poor prognosis have displayed overexpression of ubiquitous mitochondrial creatine kinase which is linked to high energy turnover and inability to remove cancer cells through apoptosis.
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Synonyms
Creatine kinase mitochondrial 1A, creatine kinase mitochondrial 1 (ubiquitous), creatine kinase U-type mitochondrial, Acidic-type mitochondrial creatine kinase, Ubiquitous mitochondrial creatine kinase, CKMT1, U-MtCK, mia-CK, EC 2.7.3, EC 2.7.3.2.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human CKMT1A mAb, clone PAT17A2AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human CKMT1A protein 40-417 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG2b heavy chain and k light chain.
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Clone
PAT17A2AT.
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Applications
The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
CKMT1A antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CYTL1 HumanDescription:
Cytokine-Like 1 Human Recombinant
Cytokine-like protein 1, Protein C17, CYTL1, C4orf4, C17.
Product # :
CYT-775Price :
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Shipping Method :
Shipped at Room temp
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Description
CYTL1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 23-136) containing 124 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 14.6kDa (calculated).
Source
Escherichia Coli.
Formulation
CYTL1 was filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Cytokine-like protein 1 (CYTL1) is a secreted protein. CYTL1 is expressed in CD34+ cell populations of bone marrow and cord blood which function as hematopoietic stem/progenitor cells. However, CYTL1 is not expressed in CD34- cells. Experiments with knock-out mice (Cytl1-/-) propose that CYTL1 is essential for the maintenance of cartilage homeostasis rather than cartilage and bone development, and loss of CYTL1 function is linked with experimental osteoarthritic cartilage destruction in mice.
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Synonyms
Cytokine-like protein 1, Protein C17, CYTL1, C4orf4, C17.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. CYTL1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHASTPPTCYSRMR ALSQEITRDF NLLQVSEPSE PCVRYLPRLY LDIHNYCVLD KLRDFVASPP CWKVAQVDSL KDKARKLYTI MNSFCRRDLV FLLDDCNALE YPIPVTTVLP DRQR.
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Background
Title: Cytokine-Like 1 Human Recombinant: Exploring its Role in Immune Regulation and Therapeutic Potential
Abstract:
Cytokine-like 1 (CYTL1) is an emerging cytokine that exhibits pleiotropic effects on immune regulation and tissue homeostasis. This research paper provides a comprehensive analysis of human recombinant CYTL1, focusing on its production, characterization, and potential applications in immune modulation. The paper highlights the significance of CYTL1 in immune cell function, inflammation, and tissue repair. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant CYTL1 in various pathological conditions. The information presented in this paper aims to enhance our understanding of human recombinant CYTL1 and its utility as a research tool and a potential immunotherapeutic agent.Introduction:
Cytokine-like 1 (CYTL1) is a recently discovered cytokine with diverse biological functions, including immune regulation and tissue repair. Human recombinant CYTL1, produced through genetic engineering techniques, provides researchers with a valuable tool to study its biological activities and explore its therapeutic potential.Production and Characterization:
Recombinant CYTL1 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CYTL1.Role in Immune Regulation:
CYTL1 has been shown to modulate immune cell function and inflammation. It can influence the differentiation and activation of various immune cell subsets, including T cells and macrophages. Recombinant CYTL1 serves as a valuable tool for investigating the mechanisms underlying immune regulation and exploring its potential as an immunomodulatory agent.Therapeutic Implications:
The dysregulation of immune responses is associated with numerous pathological conditions, including autoimmune diseases and chronic inflammation. Recombinant CYTL1 holds promise as a potential immunotherapeutic agent due to its ability to modulate immune cell function and regulate inflammatory processes. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant CYTL1 in various diseases, including autoimmune disorders and tissue regeneration.Conclusion:
Human recombinant CYTL1 is a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in immune regulation contribute to our understanding of immune responses and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant CYTL1 offer promising avenues for improving outcomes in autoimmune diseases, chronic inflammation, and tissue repair.What is the molecular weight/Mw of CYTL1 Protein?
CYTL1 Protein has a total Mw of 14.6kDa.
What is the source or expression system of CYTL1 Protein?
Escherichia Coli.
What is the Purity of CYTL1 Protein?
CYTL1 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CYTL1 Protein?
The biological functionality of CYTL1 Protein will be determined in the future.
What is the amino acid sequence of CYTL1 Protein?
MKHHHHHHASTPPTCYSRMR ALSQEITRDF NLLQVSEPSE PCVRYLPRLY LDIHNYCVLD KLRDFVASPP CWKVAQVDSL KDKARKLYTI MNSFCRRDLV FLLDDCNALE YPIPVTTVLP DRQR.
What applications can CYTL1 Protein be used in?
CYTL1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CYTL1 Protein?
The endotoxin level is minimal, CYTL1 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 12 p35 HumanDescription:
Interleukin-12 p35 Human Recombinant
NKSF1, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 35 kDa subunit (CLMF p35), TSF, Edodekin-alpha, IL-12 p35, IL-12A, IL-12 subunit p35, NK cell stimulatory factor chain 1, SGT2, FLJ39002.
Product # :
CYT-487Price :
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Shipped with Ice Packs
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Description
Interleukin-12 p35 His Human Recombinant produced in E.Coli is single, a non-glycosylated, polypeptide chain containing 197 amino acids fragment (57-253) with an amino-terminal hexahistidine tag. The IL-12 p35 His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Interleukin-12 p35 His-Tag is supplied in 1xPBS and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Active IL-12 is a p70 disulphide-linked dimer composed of p35 and p40 subunits. The protein is a pleiotropic cytokine produced primarily by antigen presenting cells and has multiple effects on T lymphocytes and natural killer cells in terms of stimulating cytotoxicity, proliferation, production of other cytokines and Th1 subset differentiation.
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Synonyms
NKSF1, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 35 kDa subunit (CLMF p35), TSF, Edodekin-alpha, IL-12 p35, IL-12A, IL-12 subunit p35, NK cell stimulatory factor chain 1, SGT2, FLJ39002.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
IL 22 RatDescription:
Interleukin-22 Rat Recombinant
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
Product # :
CYT-173Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
IL-22 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16.6kDa.The IL22 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity is measured by its ability to induce IL-10 secretion in COLO 205 (human colon carcinoma cells). The expected ED50 for this effect is 0.15-0.75ng/ml.More Info
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Introduction
IL-22 is a member of the IL-10 family of regulatory cytokines.Members of this family share partial homology in their amino acid sequences, but they are dissimilar in their biological functions. Produced by T lymphocytes, IL-22 inhibits IL-4 production by Th2 cells, and induces acute phase reactants in the liver and pancreas. IL-22 signals through a receptor system consisting of IL-10R-beta/CRF2-4 and IL-22R, both of which are members of the class II cytokine-receptor family.
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Synonyms
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Interleukin-22 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL22 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 Interleukin -22 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
LPINSQCKLE AANFQQPYIV NRTFMLAKEA SLADNNTDVR LIGEELFRGV KAKDQCYLMK QVLNFTLEDV LLPQSDRFQP YMQEVVPFLT KLSIHLSPCH ISGDDQNIQK NVRQLKETVQ KLGESGEIKA IGELDLLFMS LRNACV.
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 :
Lungkine MouseDescription:
Lungkine (CXCL15) Mouse Recombinant
C-X-C motif chemokine 15, Lungkine, Small-inducible cytokine B15, Cxcl15, Scyb15.
Product # :
CHM-286Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Mouse Lungkine produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 142 amino acids and having a molecular mass of 16.4kDa.The CXCL15 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Lungkine protein was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 7.4 and 0.02% Tween-20.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration of 20-100 ng/ml.More Info
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Introduction
Mouse Lungkine/CXCL15 (WECHE) belongs to the ELR motif-containing CXC chemokines. The mouse Lungkine gene has been mapped to chromosome 5. The cDNA of mouse Lungkine encodes a 166 amino acids (aa) protein with a 25 aa predicted signal peptide and a 141 aa mature protein with an exceptionally long C-terminal tail which extends beyond beyond the chemokine fold. Lungkine protein is secreted into bronchoalveolar space and is involved in lung-specific neutrophils trafficking. Furthermore, studies in Lungkine knockout mice propose that Lungkine is an imperative mediator of neutrophil migration from the lung parenchyma into the airspace. In addition, Lungkine is chemotactic for bone marrow progenitor cells and modulates hematopoietic cell differentiation. By Northern blot analysis and in-situ hybridization, Lungkine transcripts have only been specifically detected in the adult and fetal lung, and its expression is up-regulated under inflammatory conditions. There is a 35% aa sequence similarity between the mouse Lungkine and the human ENA-78 and a 31% similarity with the human IL-8.
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Synonyms
C-X-C motif chemokine 15, Lungkine, Small-inducible cytokine B15, Cxcl15, Scyb15.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Lungkine although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL15 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 Lungkine 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
QELRCLCIQE HSEFIPLKLI KNIMVIFETI YCNRKEVIAV PKNGSMICLD PDAPWVKATV GPITNRFLPE DLKQKEFPPA MKLLYSVEHE KPLYLSFGRP ENKRIFPFPI RETSRHFADL AHNSDRNFLR DSSEVSLTGS DA.
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 :
GPT1 AntibodyDescription:
Anti Human Glutamate Pyruvate Transaminase 1
Product # :
ANT-778Price :
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Shipping Method :
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Description
Monoclonal antibody to glutamate-pyruvate-transaminase-1
Formulation
PBS, sodium chloride and 0.095 % NaN3 as a preservative.
Purity
Protein is >95% pure.
More Info
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
GPT1 Antibody although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
Immunoassay.
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Background
Monoclonal antibodies to Glutamate-Pyruvate Transaminase 1 (GPT/ALT1) are engineered proteins designed to bind GPT1, a key
metabolic enzyme, for applications such as Western Blotting, ELISA, and immunofluorescence. These antibodies (often Mouse IgG1) are needed to recognize liver injury/ ALT1 metabolic activity. -
Type
Mouse antibody Monoclonal.
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Purification Method
Purified monoclonal IgG1 by protein A chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CTF1 Human, HisDescription:
Cardiotrophin-1 Human Recombinant, His Tag
CTF1, CT1, CT-1, Cardiophin 1.
Product # :
CYT-436Price :
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Description
The Cardiotrophin His-Tagged Fusion Protein Human, produced in E. coli, is 22.5 kDa protein containing 200 amino acid residues of the human Cardiotrophin and 12 additional amino acid residues – His Tag (underlined).
Source
Escherichia Coli.
Formulation
CTF1 was filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.
Purity
Purity of CTF1 Human Recombinant is greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction. -
Synonyms
CTF1, CT1, CT-1, Cardiophin 1.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/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 10?g/ml. In higher concentrations the solubility of this antigen is limited. Protein is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MRGSHHHHHH GSSRREGSLE DPQTDSSVSL LPHLEAKIRQ THSLAHLLTK YAEQLLQEYV QLQGDPFGLPSFSPPRLPVA GLSAPAPSHA GLPVHERLRL DAAALAALPP LLDAVCRRQA ELNPRAPRLL RRLEDAARQA RALGAAVEAL LAALGAANRG PRAEPPAATA SAASATGVFP AKVLGLRVCG LYREWLSRTE GDLGQLLPGG SA.
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Background
What is the molecular weight/Mw of CTF1 Protein?
CTF1 Protein has a total Mw of 22.5kDa.
What is the source or expression system of CTF1 Protein?
Escherichia Coli.
What is the Purity of CTF1 Protein?
CTF1 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CTF1 Protein?
The biological functionality of CTF1 Protein will be determined in the future.
What is the amino acid sequence of CTF1 Protein?
MRGSHHHHHH GSSRREGSLE DPQTDSSVSL LPHLEAKIRQ THSLAHLLTK YAEQLLQEYV QLQGDPFGLPSFSPPRLPVA GLSAPAPSHA GLPVHERLRL DAAALAALPP LLDAVCRRQA ELNPRAPRLL RRLEDAARQA RALGAAVEAL LAALGAANRG PRAEPPAATA SAASATGVFP AKVLGLRVCG LYREWLSRTE GDLGQLLPGG SA.
What applications can CTF1 Protein be used in?
CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CTF1 Protein?
The endotoxin level is minimal, CTF1 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 :
A2LD1 HumanDescription:
AIG2-Like Domain 1 Human Recombinant
Gamma-glutamylaminecyclotransferase, GGACT, AIG2-like domain-containing protein 1, A2LD1.
Product # :
PRO-172Price :
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Description
A2LD1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 173 amino acids (1-153 a.a.) and having a molecular mass of 19.4kDa. The A2LD1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The A2LD1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Gamma-glutamylaminecyclotransferase (A2LD1) is an enzyme which converts gamma-glutamylamines to free amines and 5-oxoproline. A2LD1 demonstrates high activity toward gamma-glutamyl-epsilon-lysine, derived from the breakdown of fibrin and other proteins cross-linked by transglutaminases. A2LD1 assists in the proteolytic degradation of crosslinked fibrin by breaking down isodipeptide L-gamma-glutamyl-L-epsilon-lysine, which is a byproduct of fibrin degradation. The reaction catalyzed by the A2LD1 produces 5-oxo-L-proline and a free alkylamine.
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Synonyms
Gamma-glutamylaminecyclotransferase, GGACT, AIG2-like domain-containing protein 1, A2LD1.
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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 MALVFVYGTL KRGQPNHRVL RDGAHGSAAF RARGRTLEPY PLVIAGEHNI PWLLHLPGSG RLVEGEVYAV DERMLRFLDD FESCPALYQR TVLRVQLLED RAPGAEEPPA PTAVQCFVYS RATFPPEWAQ LPHHDSYDSE GPHGLRYNPR ENR.
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 :
METAP1D HumanDescription:
Methionyl Aminopeptidase 1D Human Recombinant
MAP1D, Metap1l, Methionine aminopeptidase 1D, mitochondrial, MAP 1D, MetAP 1D, Methionyl aminopeptidase type 1D, mitochondrial, Peptidase M 1D, METAP1D.
Product # :
ENZ-759Price :
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Shipping Method :
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Description
METAP1D Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 339 amino acids (20-335a.a) and having a molecular mass of 37.4kDa. METAP1D is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The METAP1D solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Methionyl Aminopeptidase 1D (METAP1D) is a part of the peptidase M24A family. METAP1D which is overexpressed in colon cancer cell lines participates in tumorigenesis. METAP1D eliminates methionine from the N-terminus of nascent proteins.
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Synonyms
MAP1D, Metap1l, Methionine aminopeptidase 1D, mitochondrial, MAP 1D, MetAP 1D, Methionyl aminopeptidase type 1D, mitochondrial, Peptidase M 1D, METAP1D.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSSPLNHI YLHKQSSSQQ RRNFFFRRQR DISHSIVLPA AVSSAHPVPK HIKKPDYVTT GIVPDWGDSI EVKNEDQIQG LHQACQLARH VLLLAGKSLK VDMTTEEIDA LVHREIISHN AYPSPLGYGG FPKSVCTSVN NVLCHGIPDS RPLQDGDIIN IDVTVYYNGY HGDTSETFLV GNVDECGKKL VEVARRCRDE AIAACRAGAP FSVIGNTISH ITHQNGFQVC PHFVGHGIGS YFHGHPEIWH HANDSDLPME EGMAFTIEPI ITEGSPEFKV LEDAWTVVSL DNQRSAQFEH TVLITSRGAQ ILTKLPHEA.
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 :
SCG5 HumanDescription:
Secretogranin-V Human Recombinant
7B2, SgV, P7B2, SGNE1, Secretogranin-5, Secretory granule endocrine protein I.
Product # :
PRO-467Price :
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Description
SCG5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids (27-212 a.a.) and having a molecular mass of 22 kDa. SCG5 is fused to a 8 amino acid His tag at C-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
SCG5 solution (0.5mg/ml) containing 20mM Tris-HCl pH-8, 0.1mM PMSF, 1mM DTT, 0.1M NaCl and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
SCG5 also called 7B2 protein is localized in neuroendocrine tissues. SCG5 functions as a chaperone protein for the proprotein convertase PC2 and is essential for the production of an active PC2 enzyme.
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Synonyms
7B2, SgV, P7B2, SGNE1, Secretogranin-5, Secretory granule endocrine protein I.
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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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
MYSPRTPDRV SEADIQRLLH GVMEQLGIAR PRVEYPAHQA MNLVGPQSIE GGAHEGLQHL GPFGNIPNIV AELTGDNIPK DFSEDQGYPD
PPNPCPVGKT ADDGCLENTP DTAEFSREFQ LHQHLSDPEH DYPGLGKWNK KLLYEKMKGG ERRKRRSVNP YLQGQRLDNV VAKKSVPHFS
DEDKDPELEH HHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- 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 :
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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 :
Apo D HumanDescription:
Apolipoprotein-D Human Recombinant
Apolipoprotein D, Apo-D, ApoD.
Product # :
CYT-547Price :
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Shipped at Room temp
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Description
Apolipoprotein-D Human Recombinant His Tag fusion protein at C-terminus (7 highlighted a.a.) produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 174 amino acids and having a molecular mass of 19.82kDa. The protein a.a sequence corresponds to the UniProtKB/Swiss-Prot entry P05090.The Following gene modifications were made:Trp99His, Cys116Ser, Ile118Ser, Leu120Ser amino acids exchanges were introduced at the surface of Apolipoprotein-D to enhance the protein’s solubility and another three Leu23Pro, Pro133Val, Asn134Ala amino acids exchanges which facilitate its genetic manipulation. The Apolipoprotein-D is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 1mg/ml in 4mM KH2PO4, 16mM Na2HPO4 and 115mM NaCl pH 7.5.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Apolipoprotein-D is mainly associated with high density lipoproteins in human plasma. Apolipoprotein-D is an atypical apolipoprotein and, based on its primary structure, Apolipoprotein-D is a member of the lipocalin family. Lipocalins adopt a beta-barrel tertiary structure and transport small hydrophobic ligands. Apolipoprotein-D binds cholesterol, progesterone, pregnenolone, bilirubin and arachidonic acid.
Apolipoprotein-D is expressed in numerous tissues having high levels of expression in spleen, testes and brain. Apolipoprotein-D is present at high concentrations in the cyst fluid of women with gross cystic disease of the breast, a condition associated with increased risk of breast cancer. Apolipoprotein-D accumulates in regenerating peripheral nerves and in the cerebrospinal fluid of patients with neurodegenerative conditions, such as Alzheimer's disease. Apolipoprotein-D participates in maintenance and repair within the central and peripheral nervous systems. Apolipoprotein-D is a multi-ligand, multi-functional transporter and transports a ligand from 1 cell to another within an organ, scavenge a ligand within an organ for transport to the blood or could transport a ligand from the circulation to specific cells within a tissue. -
Synonyms
Apolipoprotein D, Apo-D, ApoD.
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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.
-
Solubility
It is recommended to add deionized H2O to a working volume of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter this product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
FHLGKCPNPP VQENFDVNKY PGRWYEIEKI PTTFENGRCI QANYSLMENG KIKVLNQELR ADGTVNQIEG EATPVNLTEP AKLEVKFSWF MPSAPYHILA TDYENYALVY SCTSISQSFH VDFAWILARN VALPPETVDS LKNILTSNNI DVKKMTVTDQ VNCPKLSAHHHHHH.
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Background
Apolipoprotein-D Human Recombinant: Illuminating the Role of a Multifaceted Lipid-Binding Protein
Abstract:
Apolipoprotein-D (ApoD), a multifunctional lipid-binding protein, has emerged as a fascinating player in lipid metabolism and neuroprotection. This research paper aims to provide an insightful overview of ApoD human recombinant, exploring its physiological functions, production methods, and potential therapeutic applications. By unraveling the complexities of ApoD, we gain valuable insights into its role in lipid homeostasis and its potential as a therapeutic target for neurodegenerative diseases. This article presents a concise yet comprehensive analysis of ApoD, humanizing its significance in the context of human health.Introduction:
Understanding the intricate mechanisms underlying lipid metabolism and neuroprotection is crucial for the development of novel therapeutic strategies. ApoD, a versatile protein expressed in various tissues, offers unique insights into these areas. This paper delves into the multifaceted nature of ApoD, shedding light on its significance in lipid homeostasis and neuronal health.Structure and Function of Apolipoprotein-D:
ApoD exhibits a complex molecular structure, comprising distinct domains that facilitate its binding to lipids and other biomolecules. It engages in diverse functions, including lipid transport, antioxidant defense, and modulation of neuroinflammatory responses. The versatility of ApoD underscores its pivotal role in maintaining cellular and tissue integrity.Regulation of Apolipoprotein-D Expression:
The expression of ApoD is subject to intricate regulatory mechanisms influenced by hormonal and environmental cues. Understanding the factors governing ApoD expression provides valuable insights into its physiological roles and potential therapeutic applications.Apolipoprotein-D and Neurodegenerative Diseases:
Growing evidence implicates ApoD in neuroprotection, particularly in the context of neurodegenerative diseases. ApoD exhibits neuroprotective properties by modulating oxidative stress, lipid peroxidation, and inflammatory responses, making it an intriguing target for therapeutic interventions.Production of Apolipoprotein-D Human Recombinant:
Advanced biotechnological approaches, including recombinant DNA technology and protein expression systems, enable the production of ApoD human recombinant. These methods facilitate large-scale production, purification, and characterization of ApoD, paving the way for potential therapeutic applications.Therapeutic Potential of Apolipoprotein-D Human Recombinant:
Targeting ApoD holds promise for the development of therapeutics aimed at neurodegenerative diseases. Modulating ApoD expression or function may provide neuroprotection, enhance neuronal survival, and mitigate the progression of neurodegenerative disorders.Conclusion:
Apolipoprotein-D human recombinant represents a captivating area of research, bridging the fields of lipid metabolism and neurodegeneration. Understanding the intricate interplay between ApoD, lipid homeostasis, and neuroprotection is crucial for unraveling its full therapeutic potential. Continued investigation into the functions and mechanisms of ApoD will likely lead to novel therapeutic strategies for neurodegenerative diseases.What is the molecular weight/Mw of APO D Protein?
APO D Protein has a total Mw of 19.82kDa.
What is the source or expression system of APO D Protein?
Escherichia Coli.
What is the Purity of APO D Protein?
APO D Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of APO D Protein?
The biological functionality of APO D Protein will be determined in the future.
What is the amino acid sequence of APO D Protein?
FHLGKCPNPP VQENFDVNKY PGRWYEIEKI PTTFENGRCI QANYSLMENG KIKVLNQELR ADGTVNQIEG EATPVNLTEP AKLEVKFSWF MPSAPYHILA TDYENYALVY SCTSISQSFH VDFAWILARN VALPPETVDS LKNILTSNNI DVKKMTVTDQ VNCPKLSAHHHHHH.
What applications can APO D Protein be used in?
APO D Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for APO D Protein?
The endotoxin level is minimal, APO D 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 :
NNMT HumanDescription:
Nicotinamide N-Methyltransferase Human Recombinant
Nicotineamide N-methyltransferase, NNMT.
Product # :
ENZ-418Price :
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Shipped with Ice Packs
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Description
NNMT Human Recombinant fused with a 20 amino acid His-Tag tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing a total of 284 amino acids (1-264 a.a.) and having a molecular mass of 31.7 kDa.The NNMT is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NNMT solution contains 20mM Tris pH 8.0 & 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
NNMT is part of the family of transferases, especially those transferring one-carbon group methyltransferases. NNMT is mostly expressed in the liver, and a lower expression is seen in the kidney, lung, skeletal muscle, placenta and heart. NNMT catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is significant for biotransformation of many drugs and xenobiotic compounds. NNMT is accountable for the enzymatic activity which uses S-adenosyl methionine as the methyl donor. NNMT expression is related with tumor stage and DFS time in hepatocellular carcinoma cases. NNMT is a good candidate as a tumor marker of various kinds of cancers. NNMT serum levels have significance in the premature detection and in the management of patients with colorectal cancer.
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Synonyms
Nicotineamide N-methyltransferase, NNMT.
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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 MESGFTSKDT YLSHFNPRDY LEKYYKFGSR HSAESQILKH LLKNLFKIFC LDGVKGDLLI DIGSGPTIYQLLSACESFKE IVVTDYSDQN LQELEKWLKK EPEAFDWSPV VTYVCDLEGN RVKGPEKEEK LRQAVKQVLK CDVTQSQPLG AVPLPPADCV LSTLCLDAAC PDLPTYCRAL RNLGSLLKPG GFLVIMDALK SSYYMIGEQK FSSLPLGREA VEAAVKEAGY TIEWFEVISQ SYSSTMANNEGLFSLVARKL SRPL.
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 :
EFNB2 HumanDescription:
Ephrin- B2 Human Recombinant
Ephrin-B2, EPH-related receptor tyrosine kinase ligand 5, LERK-5, HTK ligand, HTK-L, EFNB2, EPLG5, HTKL, LERK5, MGC126226, MGC126227, MGC126228.
Product # :
PRO-937Price :
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Description
EFNB2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (28-229 a.a.) and having a molecular mass of 24.9kDa.EFNB2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
EFNB2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 200mM NaCl.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Ephrin-B2 belongs to the ephrin (EPH) family. The ephrins and EPH-related receptors contain the largest subfamily of receptor protein-tyrosine kinases and have been associated with mediating developmental events, particularly in the nervous system and in erythropoiesis. Based upon their structures and sequence relationships, ephrins are allocated into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. Ephrin-B2 binds to the EPHB4 and EPHA3 receptors.
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Synonyms
Ephrin-B2, EPH-related receptor tyrosine kinase ligand 5, LERK-5, HTK ligand, HTK-L, EFNB2, EPLG5, HTKL, LERK5, MGC126226, MGC126227, MGC126228.
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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 MGSHMIVLEP IYWNSSNSKF LPGQGLVLYP QIGDKLDIIC PKVDSKTVGQ YEYYKVYMVD KDQADRCTIK KENTPLLNCA KPDQDIKFTI KFQEFSPNLW GLEFQKNKDY YIISTSNGSL EGLDNQEGGV CQTRAMKILM KVGQDASSAG STRNKDPTRR PELEAGTNGR SSTTSPFVKP NPGSSTDGNS AGHSGNNILG SEVALFA.
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 :
EG VEGF MouseDescription:
Endocrine Gland Vascular Endothelial Growth Factor Mouse Recombinant
PK1, Prokineticin 1, EG-VEGF, Prok1, Endocrine-gland-derived vascular endothelial growth factor.
Product # :
CYT-825Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
EG-VEGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids and having a molecular mass of 9.6kDa.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS pH7.4 and 3% Trehalose.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Endocrine gland-derived vascular endothelial growth factor (EG-VEGF) induces proliferation, migration, and fenestration in capillary endothelial cells derived from endocrine glands. Its expression is induced by hypoxia and is restricted to the steroidogenic glands (ovary, testis, adrenal, and placenta). Its expression is often complementary to the expression of VEGF (MIM 192240), suggesting that these molecules function in a coordinated manner. EG-VEGF potently contracts gastrointestinal (gi) smooth muscle. Induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. Has little or no effect on a variety of other endothelial and non-endothelial cell types.
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Synonyms
PK1, Prokineticin 1, EG-VEGF, Prok1, Endocrine-gland-derived vascular endothelial growth factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EG-VEGF Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EG-VEGF 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 Endocrine Gland Vascular Endothelial Growth Factor 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
AVITGACERD IQCGAGTCCA ISLWLRGLRL CTPLGREGEE CHPGSHKIPF LRKRQHHTCP CSPSLLCSRF PDGRYRCFRD LKNANF.
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Background
What is the molecular weight/Mw of EG-VEGF Protein?
EG-VEGF Protein has a total Mw of 9.6kDa.
What is the source or expression system of EG-VEGF Protein?
Escherichia Coli.
What is the Purity of EG-VEGF Protein?
EG-VEGF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of EG-VEGF Protein?
The biological functionality of EG-VEGF Protein will be determined in the future.
What is the amino acid sequence of EG-VEGF Protein?
AVITGACERD IQCGAGTCCA ISLWLRGLRL CTPLGREGEE CHPGSHKIPF LRKRQHHTCP CSPSLLCSRF PDGRYRCFRD LKNANF.
What applications can EG-VEGF Protein be used in?
EG-VEGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EG-VEGF Protein?
The endotoxin level is minimal, EG-VEGF 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 :
NRP1 HumanDescription:
Neuropilin 1 Human Recombinant
Neuropilin-1 isoform a, NRP1, BDCA4, CD304, NP1, NRP, VEGF165R, Vascular endothelial cell growth factor 165 receptor.
Product # :
CYT-1059Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NRP1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 843 amino acids (22-856a.a.) and having a molecular mass of 94.8kDa. (Molecular size on SDS-PAGE will appear at approximately 100-150kDa).NRP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
NRP1 protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
NRP1 is a coreceptor bound on membranes to tyrosine kinase receptors for semaphorin family proteins and endothelial growth factors, it is a type one transmembrane protein. Neuropilin-1 takes part in cell survival, angiogenesis, invasion, migration, and axon guidance. the protein is a potential target for cancer therapies as it interacts with VEGF (co-receptor).
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Synonyms
Neuropilin-1 isoform a, NRP1, BDCA4, CD304, NP1, NRP, VEGF165R, Vascular endothelial cell growth factor 165 receptor.
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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
FRNDKCGDTI KIESPGYLTS PGYPHSYHPS EKCEWLIQAP DPYQRIMINF NPHFDLEDRD CKYDYVEVFD GENENGHFRG KFCGKIAPPP VVSSGPFLFI KFVSDYETHG AGFSIRYEIF KRGPECSQNY TTPSGVIKSP GFPEKYPNSL ECTYIVFAPK MSEIILEFES FDLEPDSNPP
GGMFCRYDRL EIWDGFPDVG PHIGRYCGQK TPGRIRSSSG ILSMVFYTDS AIAKEGFSAN YSVLQSSVSE DFKCMEALGM ESGEIHSDQI TASSQYSTNW SAERSRLNYP ENGWTPGEDS YREWIQVDLG LLRFVTAVGT QGAISKETKK KYYVKTYKID VSSNGEDWIT IKEGNKPVLF
QGNTNPTDVV VAVFPKPLIT RFVRIKPATW ETGISMRFEV YGCKITDYPC SGMLGMVSGL ISDSQITSSN QGDRNWMPEN IRLVTSRSGW ALPPAPHSYI NEWLQIDLGE EKIVRGIIIQ GGKHRENKVF MRKFKIGYSN NGSDWKMIMD DSKRKAKSFE GNNNYDTPEL RTFPALSTRF
IRIYPERATH GGLGLRMELL GCEVEAPTAG PTTPNGNLVD ECDDDQANCH SGTGDDFQLT GGTTVLATEK PTVIDSTIQS EFPTYGFNCE FGWGSHKTFC HWEHDNHVQL KWSVLTSKTG PIQDHTGDGN FIYSQADENQ KGKVARLVSP VVYSQNSAHC MTFWYHMSGS HVGTLRVKLR
YQKPEEYDQL VWMAIGHQGD HWKEGRVLLH KSLKLYQVIF EGEIGKGNLG GIAVDDISIN NHISQEDCAK PADLDKKNPE IKIDETGSTP GYEGEGEGDK NISRKPGNVL KTLDPLEHHH HHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CXCL5 HumanDescription:
Epithelial Neutrophil-Activating Protein 78 Human Recombinant (CXCL5)
Small inducible cytokine B5, CXCL5, Epithelial-derived neutrophil-activating protein 78, Neutrophil-activating peptide ENA-78, ENA-78(1-78), chemokine (C-X-C motif) ligand 5, SCYB5.
Product # :
CHM-331Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Epithelial Neutrophil-Activating Protein 78 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 74 amino acids and having a molecular mass of 8020 Dalton. The CXCL5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CXCL5 was lyophilized from a concentrated (1mg/ml) solution in water containing no additives.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity was determined by measuring the dose dependent mobilization of intracellular calcium (calcium flux) with human neutrophils. Significant calcium mobilization is observed with 100ng/mL (corresponding to a Specific Activity of 10,000IU/mg) of recombinant human ENA-78.More Info
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Introduction
Chemokine (C-X-C motif) ligand 5 (CXCL5) is a small cytokine belonging to the CXC chemokine family that is also known as epithelial-derived neutrophil-activating peptide 78 (ENA-78). It is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. Expression of CXCL5 has also been observed in eosinophils, and can be inhibited with the type II IFN. This chemokine stimulates the chemotaxis of neutrophils possesses angiogenic properties. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2. The gene for CXCL5 is encoded on four exons and is located on human chromosome 4 amongst several other CXC chemokine genes. CXCL5 has been implicated in connective tissue remodelling.
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Synonyms
Small inducible cytokine B5, CXCL5, Epithelial-derived neutrophil-activating protein 78, Neutrophil-activating peptide ENA-78, ENA-78(1-78), chemokine (C-X-C motif) ligand 5, SCYB5.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized ENA78 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL5 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 ENA-78 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala- Ala -Val-Leu-Arg.
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Background
What is the molecular weight/Mw of CXCL5 HUMAN Protein?
CXCL5 HUMAN Protein has a total Mw of 8.02kDa.
What is the source or expression system of CXCL5 HUMAN Protein?
Escherichia Coli.
What is the Purity of CXCL5 HUMAN Protein?
CXCL5 HUMAN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL5 HUMAN Protein?
The biological activity was determined by measuring the dose dependent mobilization of intracellular calcium (calcium flux) with human neutrophils. Significant calcium mobilization is observed with 100ng/mL (corresponding to a Specific Activity of 10,000IU/mg) of recombinant human ENA-78.
What is the amino acid sequence of CXCL5 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala- Ala -Val-Leu-Arg.
What applications can CXCL5 HUMAN Protein be used in?
CXCL5 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL5 HUMAN Protein?
The endotoxin level is minimal, CXCL5 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 :
SRI HumanDescription:
Sorcin Human Recombinant
Sorcin, 22 kDa protein, CP-22, CP22, V19, SRI, SCN, FLJ26259.
Product # :
PRO-166Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SRI Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 221 amino acids (1-198 a.a.) and having a molecular mass of 24.1kDa. The SRI is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SRI solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.2M NaCl, 1mM DTT and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Sorcin (SRI) which is a 22kDa calcium-binding protein was originally identified in multidrug-resistant cells. Sorcin, which modulates excitation-contraction coupling in the heart, contributes to calcium homeostasis in the heart sarcoplasmic reticulum.
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Synonyms
Sorcin, 22 kDa protein, CP-22, CP22, V19, SRI, SCN, FLJ26259.
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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 MGSMAYPGHP GAGGGYYPGG YGGAPGGPAF PGQTQDPLYG YFAAVAGQDG QIDADELQRC LTQSGIAGGY KPFNLETCRL MVSMLDRDMS GTMGFNEFKE LWAVLNGWRQ HFISFDTDRS GTVDPQELQK ALTTMGFRLS PQAVNSIAKR YSTNGKITFD DYIACCVKLR ALTDSFRRRD TAQQGVVNFP YDDFIQCVMS V.
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 :
ENO2 Human, HisDescription:
Enolase-2 Human Recombinant, His Tag
Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.
Product # :
ENZ-298Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Neuron Specific Enolase Human Recombinant is expressed in E. coli containing 433 amino acids 2-434 fused to an amino terminal hexahistidine tag.The NSE is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Enolase 2 is supplied in 10mM Tris-HCl (pH 8), 250mM NaCl, 0.5mM DTT, 1.5mM Cysteine, and 50% Glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Single band on Western Blot.More Info
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Introduction
NSE is the ?? isoform of the glycolytic enzyme enolase and is expressed primarily in neurons, in normal and neoplastic neuroendocrine cells. NSE is a highly soluble cytoplasmic protein that is readily secreted into the CSF and serum following tissue damage. NSE shows neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons and binds in a calcium-dependent manner to cultured neocortical neurons promoting cell survival.
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Synonyms
Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.
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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 1-2 weeks. Store, frozen at -20°C for longer periods of time. Please prevent freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
OLR1 Human, HEKDescription:
Oxidized Low Density Lipoprotein Receptor 1 Human Recombinant, HEK
Oxidized low density lipoprotein (lectin-like) receptor 1, CLEC8A, hLOX1, SCARE1, Lectin-type oxidized LDL receptor 1, Lectin-like oxidized LDL receptor 1, C-type lectin domain family 8 member A, LOXIN, SLOX1, ox LDL receptor 1, Oxidized low-density lipoprotein receptor 1 soluble form, scavenger receptor class E member 1, SR-E1.
Product # :
PRO-2293Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
OLR1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Ser61-Gln273) containing a total of 221 amino acids, having a calculated molecular mass of 25.3kDa and fused to a 8 aa Flag tag at N-Terminus.
Source
HEK 293.
Formulation
OLR1 was filtered (0.4µm) and lyophilized in phosphate buffered saline pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
OLR1 is a type II membrane protein which belongs to the C-type lectin family and performs as a cell-surface receptor for Ox-LDL. Ox-LDL has a part in early ather-osclerosis, which includes the transformation of monocyte-derived macro-phages to foam cells in atherosclerotic lesions. In addition, OLR1 protein triggers the activation of the NF?B signal transduction pathway.
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Synonyms
Oxidized low density lipoprotein (lectin-like) receptor 1, CLEC8A, hLOX1, SCARE1, Lectin-type oxidized LDL receptor 1, Lectin-like oxidized LDL receptor 1, C-type lectin domain family 8 member A, LOXIN, SLOX1, ox LDL receptor 1, Oxidized low-density lipoprotein receptor 1 soluble form, scavenger receptor class E member 1, SR-E1.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Filter sterilize your culture media/working solutions containing this non-sterile product before using in cell culture.
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Amino Acid Sequence
DYKDDDDKSQ VSDLLTQEQA NLTHQKKKLE GQISARQQAE EASQESENEL KEMIETLARK LNEKSKEQME LHHQNLNLQE TLKRVANCSA PCPQDWIWHG ENCYLFSSGS FNWEKSQEKC LSLDAKLLKI NSTADLDFIQ QAISYSSFPF WMGLSRRNPS YPWLWEDGSP LMPHLFRVRG AVSQTYPSGT CAYIQRGAVY AENCILAAFS ICQKKANLRA Q.
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.