Search results
598 results found for “Mitochondrial Transcription Factor”
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Name :
Leptin ChickenDescription:
Leptin Chicken Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-505Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Chicken Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 145 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its activity is however 5-10 fold lower as compared to mammalian leptins.More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin 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-Val-Pro-Cys-Gln.
Recombinant Chicken leptin was produced according to the a.a. sequence published by the groups of Taouis & McMutry, see Raver et al. Protein Expr Purif. 1998 Dec; 14(3):403-8.
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Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.19 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC,using calibrated solution of Leptin Chicken as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
KGF Human, PlantDescription:
Keratinocyte Growth Factor Human Recombinant, Plant
HBGF-7, FGF7, FGF-7, KGF.
Product # :
CYT-1212Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
KGF Human Recombinant produced in Oryza Sativa is a single, polypeptide chain having a molecular mass of approximately 19.2kDa. The KGF is purified by proprietary chromatographic techniques.
Source
Rice Grain
Formulation
Lyophilized KGF from a 0.2μm filtered solution containing no stabilizers.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
KGF has full biological activity when compared to standards. The activity is determined by the dose-dependent proliferation of HUVECs and is typically 10ng/ml corresponding to a specific activity of 100,000U/mg.
More Info
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Introduction
KGF is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF7 is a potent epithelial cell-specific growth factor, whose mitogenic activity is predominantly exhibited in keratinocytes but not in fibroblasts and endothelial cells. Studies of mouse and rat homologs of this gene implicated roles in morphogenesis of epithelium, reepithelialization of wounds, hair development and early lung organogenesis.
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Synonyms
HBGF-7, FGF7, FGF-7, KGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized KGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF7 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 KGF in sterile 18MΩ-cm at 100µg/ml, which can then be further diluted to other aqueous solutions.
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 :
FOSL2 HumanDescription:
FOS-Like Antigen 2 Human Recombinant
FOS-Like Antigen 2, FRA-2, FRA2, Fos-Related Antigen 2, FOSL2.
Product # :
PRO-2173Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FOSL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 349 amino acids (1-326 a.a) and having a molecular mass of 37.6kDa.FOSL2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FOSL2 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH 8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
FOS-Like Antigen 2, also known as FOSL2 is a protein which is encoded in humans by the FOSL2 gene. The Fos gene family consists of four members: FOS, FOSB, FOSL1, and FOSL2. Furthermore, these genes encode leucine zipper proteins which can dimerize with proteins of the JUN family, in that way forming the transcription factor complex AP-1. As such, the FOS proteins have been involved as regulators of cell proliferation, differentiation, as well transformation.
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Synonyms
FOS-Like Antigen 2, FRA-2, FRA2, Fos-Related Antigen 2, FOSL2.
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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 MGSMYQDYPG NFDTSSRGSS GSPAHAESYS SGGGGQQKFR VDMPGSGSAF IPTINAITTS QDLQWMVQPT VITSMSNPYP RSHPYSPLPG LASVPGHMAL PRPGVIKTIG TTVGRRRRDE QLSPEEEEKR RIRRERNKLA AAKCRNRRRE LTEKLQAETE ELEEEKSGLQ KEIAELQKEK EKLEFMLVAH GPVCKISPEE RRSPPAPGLQ PMRSGGGSVG AVVVKQEPLE EDSPSSSSAG LDKAQRSVIK PISIAGGFYG EEPLHTPIVV TSTPAVTPGT SNLVFTYPSV LEQESPASPS ESCSKAHRRS SSSGDQSSDS LNSPTLLAL
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 :
NUDT9 HumanDescription:
Nudix Type Motif 9 Human Recombinant
ADP-ribose pyrophosphatase mitochondrial, ADP-ribose diphosphatase, ADP-ribose phosphohydrolase, Adenosine diphosphoribose pyrophosphatase, ADPR-PPase, Nucleoside diphosphate-linked moiety X motif 9, Nudix motif 9, NUDT9, NUDT10, PSEC0099, UNQ3012/PRO9771.
Product # :
ENZ-137Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NUDT9 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 325 amino acids (47-350 a.a.) and having a molecular mass of 36.5kDa (molecular weight on SDS-PAGE will appear higher).NUDT9 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NUDT9 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 1mM DTT and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
NUDT9 is a member of a superfamily of Nudix hydrolases. NUDT9 functions as a highly specific adenosine diphosphate ribose pyrophosphatase which hydrolyzes ADP ribose to AMP and ribose 5'-phosphate. In addition, NUDT9 may be involved in the regulation of the menstrual cycle and may be related to the proliferation of glandular cells in the human endometrium.
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Synonyms
ADP-ribose pyrophosphatase mitochondrial, ADP-ribose diphosphatase, ADP-ribose phosphohydrolase, Adenosine diphosphoribose pyrophosphatase, ADPR-PPase, Nucleoside diphosphate-linked moiety X motif 9, Nudix motif 9, NUDT9, NUDT10, PSEC0099, UNQ3012/PRO9771.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
NUDT9 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MNTNVMSGSN GSKENSHNKA RTSPYPGSKV ERSQVPNEKV GWLVEWQDYK PVEYTAVSVL AGPRWADPQI SESNFSPKFN EKDGHVERKS KNGLYEIENG RPRNPAGRTG LVGRGLLGRW GPNHAADPII TRWKRDSSGN KIMHPVSGKH ILQFVAIKRK DCGEWAIPGG MVDPGEKISA TLKREFGEEA LNSLQKTSAE KREIEEKLHK LFSQDHLVIY KGYVDDPRNT DNAWMETEAV NYHDETGEIM DNLMLEAGDD AGKVKWVDIN DKLKLYASHS QFIKLVAEKR DAHWSEDSEA DCHAL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
EGF Rat ProteinDescription:
Epidermal Growth Factor Rat
Urogastrone, URG, EGF.
Product # :
CYT-556Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Epidermal Growth Factor Rat purified from submandibular gland is a single, glycosylated, polypeptide chain having a molecular mass of 6.15 kDa.The EGF is purified by proprietary chromatographic techniques.
Source
Adult Male Rat Submandibular Glands.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.01M sodium acetate buffer.
Purity
Greater than 99.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. -
Synonyms
Urogastrone, URG, EGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 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 Epidermal 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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Background
Illuminating Epidermal Growth Factor Rat Recombinant: Deciphering Cellular Signaling and Therapeutic Potential
Abstract:
This research paper delves into the enigmatic realm of Epidermal Growth Factor Rat Recombinant (EGF-RR), unraveling its intricate molecular attributes, signaling cascades, and therapeutic prospects. By employing cutting-edge methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the multifaceted interplay between EGF-RR and cellular responses, offering novel avenues for therapeutic interventions.
Introduction:
Epidermal Growth Factor (EGF) is pivotal in cellular regulation. This paper navigates the complexities of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and potential therapeutic applications.
Protein Expression and Purification:
The study embarks on precise gene optimization to enhance EGF-RR expression. Purification techniques like affinity chromatography yield purified EGF-RR, primed for subsequent analyses.
Receptor Binding Assays and Ligand Interaction:
Employing advanced receptor binding assays, the paper deciphers EGF-RR's engagement with its cognate receptor. Quantitative assessments uncover binding kinetics, shedding light on the intricacies of EGF-RR's molecular interaction.
Cellular Signaling Pathways and Responses:
In vitro cellular assays unveil the signaling cascades ignited by EGF-RR. Through quantitative phosphoproteomic profiling, the study unravels phosphorylation events triggered by EGF-RR, delineating its role in cellular proliferation, migration, and differentiation.
Bioinformatics Insights and Structural Modeling:
Bioinformatics tools facilitate molecular dynamics simulations, offering insights into EGF-RR's receptor interactions and downstream signaling pathways. Structural modeling captures EGF-RR's conformational changes during signaling cascades.
Therapeutic Implications and Future Prospects:
EGF-RR's intricate signaling dynamics open avenues for therapeutic exploration. Harnessing its potential in wound healing, tissue regeneration, and cancer modulation emerges as a promising avenue for precision medicine.
Challenges and Future Directions:
Challenges, including context-specific responses, beckon further investigation. Future research should delve into cross-talk between signaling pathways and EGF-RR's contributions to diverse disease contexts.
Conclusion:
A fusion of advanced methodologies and visionary insights unveils Epidermal Growth Factor Rat Recombinant as an intriguing subject. Its molecular intricacies and complex cellular interplay ignite prospects for therapeutic breakthroughs, ushering in a new era of precision medicine.
What is the molecular weight/Mw of EGF RAT Protein?
EGF RAT Protein has a total Mw of 6.15kDa.
What is the source or expression system of EGF RAT Protein?
Adult Male Rat Submandibular Glands.
What is the Purity of EGF RAT Protein?
EGF RAT Protein is >99% pure as determined by SDS-PAGE.
What is the Biological Activity of EGF RAT Protein?
The biological functionality of EGF RAT Protein will be determined in the future.
What is the amino acid sequence of EGF RAT Protein?
EGF RAT Protein is composed from 53 amino acids.
What applications can EGF RAT Protein be used in?
EGF RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EGF RAT Protein?
The endotoxin level is minimal, EGF RAT 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 :
SNAPC1 HumanDescription:
Small Nuclear RNA Activating Complex, Polypeptide 1 Human Recombinant
PTFgamma, SNAP43, snRNA-activating protein complex subunit 1, SNAPc subunit 1, Proximal sequence element-binding transcription factor subunit gamma, PSE-binding factor subunit gamma, PTF subunit gamma, Small nuclear RNA-activating complex polypeptide 1, SNAPc 43 kDa subunit, SNAPC1.
Product # :
PRO-2085Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SNAPC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 391 amino acids (1-368 a.a) and having a molecular mass of 45.4kDa.SNAPC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SNAPC1 protein solution (1mg/ml) contains 20mM Tris-HCl (pH 8.0) and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Small Nuclear RNA Activating Complex, Polypeptide 1 (SNAPC1) is a part of the SNAPc complex necessary for the transcription of both RNA polymerase II and III small-nuclear RNA genes. SNAPC1 binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Moreover, SNAPC1 recruits TBP and BRF2 to the U6 snRNA TATA box.
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Synonyms
PTFgamma, SNAP43, snRNA-activating protein complex subunit 1, SNAPc subunit 1, Proximal sequence element-binding transcription factor subunit gamma, PSE-binding factor subunit gamma, PTF subunit gamma, Small nuclear RNA-activating complex polypeptide 1, SNAPc 43 kDa subunit, SNAPC1.
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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 MGSMGTPPGL QTDCEALLSR FQETDSVRFE DFTELWRNMK FGTIFCGRMR NLEKNMFTKE ALALAWRYFL PPYTFQIRVG ALYLLYGLYN TQLCQPKQKI RVALKDWDEV LKFQQDLVNA QHFDAAYIFR KLRLDRAFHF TAMPKLLSYR MKKKIHRAEV TEEFKDPSDR VMKLITSDVL EEMLNVHDHY QNMKHVISVD KSKPDKALSL IKDDFFDNIK NIVLEHQQWH KDRKNPSLKS KTNDGEEKME GNSQETERCE RAESLAKIKS KAFSVVIQAS KSRRHRQVKL DSSDSDSASG QGQVKATRKK EKKERLKPAG RKMSLRNKGN VQNIHKEDKP LSLSMPVITE EEENESLSGT EFTASKKRRK H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MAFK AntibodyDescription:
V-maf Musculoaponeurotic Fibrosarcoma Oncogene K, Mouse Anti Human
NFE2U, P18, Erythroid transcription factor NF-E2 p18 subunit, MAFK, Transcription factor MafK.
Product # :
ANT-463Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
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Introduction
MAFK is a member of the bZIP family and Maf subfamily. Members from Maf family of basic region/leucine zipper (bZIP) transcription factors influence transcription in a positive or negative way, depending on their protein associate and the context of the target promoter. Small Mafs act as transcriptional repressors when they dimerize among themselves. Yet, they seem to function as transcriptional activators by dimerizing with other basic-zipper proteins and employing them to specific DNA-binding sites.
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Synonyms
NFE2U, P18, Erythroid transcription factor NF-E2 p18 subunit, MAFK, Transcription factor MafK.
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Physical Appearance
Sterile Filtered colorless solution.
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Immunogen
Anti-human MAFK mAb, clone PAT2F7A, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human MAFK protein 1-156 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG2a heavy chain and Kappa light chain.
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Clone
PAT2F7A.
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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
MAFK 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 :
EGF Long HumanDescription:
Epidermal Growth Factor Long Human Recombinant
Urogastrone, URG, EGF.
Product # :
CYT-798Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Human EGF Long produced in E.coli cells is a single non-glycosylated, polypeptide chain containing 106 amino acids and having a molecular mass of 12.3kDa. The EGF Long is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EGF Long was lyophilized from a 0.2µm filtered concentrated solution in 10mM HCl.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 106 IU/mg.More Info
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Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Long EGF is a recombinant analog of Human EGF developed as a replacement for use in therapeutic cell culture applications as a like-for-like supplement for Recombinant Human or native EGF. It includes the Human EGF amino acid sequence plus a 53 amino acid N-terminal extension peptide.
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Synonyms
Urogastrone, URG, EGF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EGF Long although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF Long 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 EGF Long in sterile 100mM AcOH (acetic Acid) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MFPAMPLSSL FANAVLRAQH LHQLAADTYK EFERAYIPEG QRYSIQVNFA HYGNSDSECP LSHDGYCLHD GVCMYIEALD KYACNCVVGY IGERCQYRDL KWWELR
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Background
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 12.3kDa.
What is the source or expression system of EGF Protein?
Escherichia Coli.
What is the Purity of EGF Protein?
EGF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of EGF Protein?
The ED50 as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 ng/ml, corresponding to a specific activity of > 1.0 × 106 IU/mg.
What is the amino acid sequence of EGF Protein?
MFPAMPLSSL FANAVLRAQH LHQLAADTYK EFERAYIPEG QRYSIQVNFA HYGNSDSECP LSHDGYCLHD GVCMYIEALD KYACNCVVGY IGERCQYRDL KWWELR
What applications can EGF Protein be used in?
EGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, EGF 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 :
GM- CSF HumanDescription:
Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, MGC131935, MGC138897.
Product # :
CYT-221Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Granulocyte Macrophage Colony Stimulating Factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids and having a molecular mass of 14477 Dalton. GM-CSF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GM-CSF was lyophilized after extensive dialysis against 2mM sodium phosphate buffer pH= 7.4±0.1.
Purity
Greater than 98.0% as determined by:
1. Analysis by RP-HPLC.
2. Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.1 ng/ml, corresponding to a Specific Activity of 11,100,000 IU/mg.More Info
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Introduction
Granulocyte Macrophage Colony Stimulating Factor (GM-CSF) was first characterized as a growth factor that supports the in-vitro colony formation of granulocytes-macrophages progenitor cells. It is a pleiotropic cytokine and a member of a family of endogenous cytokines of the hematopoietic system. GM-CSF is produced as a response to immune or inflammatory stimuli by activated cells of the hematopoietic system such as T cells, B cells, macrophages, mast cells and also fibroblasts and alveolar epithelial cells. It plays an important role in regulating the proliferation, differentiation, survival and activation of hematopoietic cells such as granulocytes and monocytes ,neutrophiles, basophiles and eosonophoiles, erythroid cells, megakaryocytes and T cells.
Human and mouse GM-CSF have about 56% homology and are species specific. Human GM-CSF is not active on mouse cells and vice versa. It is active on canine and feline cells.
GMCSF is 144 amino acids, 22kDa glycoprotein. It is composed of four bundles alpha helices. Its receptor is heterodimers with a ligand-specific alpha subunit and a betac subunit that is shared with the interleukin IL-3 and IL-5 receptors. This unusual form of receptor assembly likely applies also to IL-3 and IL-5 receptors. Cross-linking the two receptor subunits is required for receptor activation and signaling .
GMCSF has been shown to be involved in maturation, mobilization and antigen presentation of myeloid dentritic cells (DCs) in-vivo or ex-vivo. This function promotes Th1 immune responses, cytotoxcity, anti-angiogenesis as well as allergic inflammation, and the development of autoimmunity. Therefore GMCSF can be used in immunotherapy for the treatment of immune suppressed and immune-compromised patients as well as in veterinary medicine for the same purpose. GM-CSF is also important in regulation of embryo development and pregnancy and specifically in embryo implantation and subsequent development . -
Synonyms
CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, MGC131935, MGC138897.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF 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 Granulocyte Macrophage Colony Stimulating 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
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.
N-terminal methionine has been completely removed enzymatically. -
Background
What is the molecular weight/Mw of GM CSF HUMAN Protein?
GM CSF HUMAN Protein has a total Mw of 14.47kDa.
What is the source or expression system of GM CSF HUMAN Protein?
Escherichia Coli.
What is the Purity of GM CSF HUMAN Protein?
GM CSF HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of GM CSF HUMAN Protein?
The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.1 ng/ml, corresponding to a Specific Activity of 11,100,000 IU/mg.
What is the amino acid sequence of GM CSF HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.
N-terminal methionine has been completely removed enzymatically.
What applications can GM CSF HUMAN Protein be used in?
GM CSF HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GM CSF HUMAN Protein?
The endotoxin level is minimal, GM CSF HUMAN Protein was purified using conventional chromatography techniques.
-
Protein content
GM-CSF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.963 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GEN computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of GM-CSF as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
HES7 HumanDescription:
Hairy and Enhancer of Split 7 Human Recombinant
Hairy and enhancer of split 7, bHLHb37, SCDO4, Transcription factor HES-7, HES7, hHes7, Class B basic helix-loop-helix protein 37, bHLH factor Hes7.
Product # :
PRO-1306Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HES7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 253 amino acids (1-230) and having a molecular mass of 27kDa. HES7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HES7 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
HES7 belongs to the Hairy and enhancer of split family of bHLH transcription factors. The mouse ortholog of the HES7 is set by Notch signaling. The protein serves as a transcriptional repressor, and is involved in correct patterning of the axial skeleton. A mutation in HES7 has been shown to result in spondylocostal dysostosis. Multiple transcript variants encoding different isoforms have been discovered for HES7.
-
Synonyms
Hairy and enhancer of split 7, bHLHb37, SCDO4, Transcription factor HES-7, HES7, hHes7, Class B basic helix-loop-helix protein 37, bHLH factor Hes7.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMVTRDRA ENRDGPKMLK PLVEKRRRDR INRSLEELRL LLLERTRDQN LRNPKLEKAE ILEFAVGYLR ERSRVEPPAA AAPGVPRSPV QDAEALASCY LSGFRECLLR LAAFAHDASP AARAQLFSAL HGYLRPKPPR PKPVDPRPPA PRPSLDPAAP ALGPALHQRP PVHQGHPSPR CAWSPSLCSP RAGDSGAPAP LTGLLPPPPP PHRQDGAPKA PLPPPPAFWR PWP.
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 :
EGF RatDescription:
Epidermal Growth Factor Rat Recombinant
Urogastrone, URG, EGF.
Product # :
CYT-669Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
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Description
Epidermal Growth Factor Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6151 Dalton. The Rat EGF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Rat EGF was lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in PBS, pH 7.4.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells is less than 0.1ng/ml, corresponding to a specific activity of > 10,000,000 units/mg.More Info
-
Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. -
Synonyms
Urogastrone, URG, EGF.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Rat EGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat EGF should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Rat EGF in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
NSNTGCPPSY DGYCLNGGVC MYVESVDRYV CNCVIGYIGE RCQHRDLRWW KLR.
-
Background
Pioneering Insights into Epidermal Growth Factor Rat Recombinant: Unraveling Signaling Dynamics and Therapeutic Implications
Abstract:
This research paper delves into the unexplored landscape of Epidermal Growth Factor Rat Recombinant (EGF-RR), delving into its intricate molecular attributes, signaling pathways, and potential therapeutic applications. By employing advanced methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the complex interplay between EGF-RR and cellular responses, offering a new perspective for therapeutic interventions.
Introduction:
Epidermal Growth Factor (EGF) holds a key role in cellular regulation. This paper navigates the intricacies of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and its potential therapeutic implications.
Protein Expression and Purification:
The paper delves into the meticulous engineering of EGF-RR, involving gene optimization for enhanced expression. Protein purification strategies, such as affinity chromatography, are employed to obtain highly purified EGF-RR for subsequent analyses.
Receptor Binding Assays and Ligand Interaction:
Advanced receptor binding assays elucidate the interaction of EGF-RR with its cognate receptor. By quantifying binding affinities and kinetic rates, the study unveils the nuances of EGF-RR's engagement with its receptor, shedding light on potential structural determinants.
Cellular Signaling Pathways and Functional Responses:
Through in vitro cellular assays, the study unravels the intricate signaling pathways initiated by EGF-RR. Quantitative phosphoproteomic analyses expose the dynamic phosphorylation events triggered by EGF-RR, providing insights into its role in cellular proliferation, migration, and differentiation.
Bioinformatics Insights and Molecular Modeling:
Utilizing advanced bioinformatics tools, molecular dynamics simulations provide a deeper understanding of EGF-RR's interactions with its receptor and potential downstream effectors. Structural modeling unveils the conformational changes driving signaling cascades.
Therapeutic Prospects and Novel Avenues:
The molecular insights into EGF-RR's signaling dynamics open avenues for therapeutic exploration. Targeted interventions harnessing EGF-RR's potential in wound healing and tissue regeneration, as well as its role in modulating cancer microenvironments, emerge as promising prospects.
Challenges and Future Directions:
Despite progress, challenges such as deciphering context-dependent signaling responses remain. Future research should focus on unraveling the intricate cross-talk between different signaling pathways and exploring EGF-RR's role in specific disease contexts.
Conclusion:
In a convergence of advanced methodologies and visionary insights, Epidermal Growth Factor Rat Recombinant emerges as a captivating subject. Its distinctive molecular attributes and complex cellular interplay offer potential avenues for therapeutic interventions, ushering in a new era of precision medicine.
What is the molecular weight/Mw of EGF RAT Protein?
EGF RAT Protein has a total Mw of 6.1kDa.
What is the source or expression system of EGF RAT Protein?
Escherichia Coli.
What is the Purity of EGF RAT Protein?
EGF RAT Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EGF RAT Protein?
The ED50 as calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells is less than 0.1ng/ml, corresponding to a specific activity of > 10,000,000 units/mg.
What is the amino acid sequence of EGF RAT Protein?
NSNTGCPPSY DGYCLNGGVC MYVESVDRYV CNCVIGYIGE RCQHRDLRWW KLR.
What applications can EGF RAT Protein be used in?
EGF RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EGF RAT Protein?
The endotoxin level is minimal, EGF RAT 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 :
HINT2 HumanDescription:
Histidine Triad Nucleotide Binding Protein 2 Human Recombinant
Histidine triad nucleotide-binding protein 2 mitochondrial, HINT-2, HINT-3 HIT-17kDa, PKCI-1-related HIT protein, HINT2, histidine triad nucleotide binding protein 2, HIT-17.
Product # :
PRO-1455Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
HINT2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (18-163 a.a) and having a molecular mass of 17.9kDa.HINT2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HINT2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Histidine triad nucleotide-binding protein 2 (HINT2) belongs to the triad proteins, which are nucleotide hydrolases and transferases that act on the alpha-phosphate of ribonucleotides. Hydrolase is most likely involved in steroid biosynthesis, furthermore it might play a role in apoptosis. HINT2 shows high expression in liver and pancreas. Expression is significantly down-regulated in hepatocellular carcinoma (HCC) patients.
-
Synonyms
Histidine triad nucleotide-binding protein 2 mitochondrial, HINT-2, HINT-3 HIT-17kDa, PKCI-1-related HIT protein, HINT2, histidine triad nucleotide binding protein 2, HIT-17.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSVAATGVR GGQVRGAAGV TDGNEVAKAQ QATPGGAAPT IFSRILDKSL PADILYEDQQ CLVFRDVAPQ APVHFLVIPK KPIPRISQAE EEDQQLLGHL LLVAKQTAKA EGLGDGYRLV INDGKLGAQS VYHLHIHVLG GRQLQWPPG.
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 :
FGF6 HumanDescription:
Fibroblast Growth Factor-6 Human Recombinant
Fibroblast Growth Factor 6, Heparin Secretory-Transforming Protein 2, Heparin-Binding Growth Factor 6, HBGF-6, HSTF-2, FGF-6, HST-2, HST2, HSTF2, FGF6.
Product # :
CYT-979Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
FGF6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain having containing 169 amino acids and having a molecular mass of 18.9kDa.The FGF-6 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FGF-6 protein was lyophilized from a 0.2µm filtered solution in 10mM sodium phosphate and 50mM sodium chloride pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Fibroblast Growth Factor-6 (FGF6) belongs to the fibroblast growth factor (FGF) family. FGF family members possess extensive mitogenic and cell survival functions, and are involved in various biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. The FGF6 gene displayes oncogenic transforming activity when transfected into mammalian cells. The mouse homolog of the FGF6 gene displays a restricted expression profile predominantly in the myogenic lineage, suggesting a role in muscle regeneration or differentiation.
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Synonyms
Fibroblast Growth Factor 6, Heparin Secretory-Transforming Protein 2, Heparin-Binding Growth Factor 6, HBGF-6, HSTF-2, FGF-6, HST-2, HST2, HSTF2, FGF6.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized FGF6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-6 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized FGF6 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MGTRANNTLL DSRGWGTLLS RSRAGLAGEI AGVNWESGYL VGIKRQRRLY CNVGIGFHLQ VLPDGRISGT HEENPYSLLE ISTVERGVVS LFGVRSALFV AMNSKGRLYA TPSFQEECKF RETLLPNNYN AYESDLYQGT YIALSKYGRV KRGSKVSPIM TVTHFLPRI.
-
Background
What is the molecular weight/Mw of FGF6 Protein?
FGF6 Protein has a total Mw of 18.9kDa.
What is the source or expression system of FGF6 Protein?
Escherichia Coli.
What is the Purity of FGF6 Protein?
FGF6 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF6 Protein?
The biological functionality of FGF6 Protein will be determined in the future.
What is the amino acid sequence of FGF6 Protein?
MGTRANNTLL DSRGWGTLLS RSRAGLAGEI AGVNWESGYL VGIKRQRRLY CNVGIGFHLQ VLPDGRISGT HEENPYSLLE ISTVERGVVS LFGVRSALFV AMNSKGRLYA TPSFQEECKF RETLLPNNYN AYESDLYQGT YIALSKYGRV KRGSKVSPIM TVTHFLPRI.
What applications can FGF6 Protein be used in?
FGF6 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF6 Protein?
The endotoxin level is minimal, FGF6 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 :
PDGF-BB EquineDescription:
Platelet Derived Growth Factor-BB Equine Recombinant
Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.
Product # :
CYT-1199Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
PDGF-BB Equine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide dimer chain containing 2 x 110 amino acids and having a total molecular mass of 24.8kDa.The PDGF-BB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a sterile (0.2µ) filtered solution containing 10 mM sodium phosphate, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by 3T3 proliferation is ≤ 30 ng/mL, corresponding to a specific activity of ≥ 3.3 x 10^4 units/mg.
More Info
-
Introduction
PDGF-BB is a member of the platelet-derived growth factor family. The four members of this family are mitogenic factors for cells of mesenchymal origin and are characterized by a motif of eight cysteines. This gene product can exist either as a homodimer (PDGF-BB) or as a heterodimer with the platelet-derived growth factor alpha polypeptide (PDGF-AB), where the dimers are connected by disulfide bonds. Mutations in this gene are associated with meningioma. Reciprocal translocations between chromosomes 22 and 7, at sites where this gene and that for COL1A1 are located, are associated with a particular type of skin tumor called dermatofibrosarcoma protuberans resulting from unregulated expression of growth factor. Two splice variants have been identified for this gene.
-
Synonyms
Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized PDGF-BB although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF-BB Human should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized PDGF-BB in sterile water at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MSLGSLAVAE PAMIAECKTR TEVFEISRRL IDRTNANFLV WPPCVEVQRC SGCCNNRHVQ CRPTQVQLRP VQVRKIEIVR KKPTFKKATV TLEDHLACKC ETVGAARPVT
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 :
FIS1 HumanDescription:
Fission-1 Human Recombinant
TTC11, Tetratricopeptide repeat domain 11, Fission 1 (mitochondrial outer membrane) homolog (S. cerevisiae).
Product # :
PRO-829Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FIS1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 142 amino acids (1-122 a.a.) and having a molecular mass of 16.3 kDa. FIS1 protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
FIS1 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8 and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
FIS1 is part of the mitochondrial complex that promotes mitochondrial fission. FIS1 induces cytochrome C discharge from the mitochondrion to the cytosol, eventually leading to apoptosis. FIS1 participates in peroxisomal growth and division. The C terminus is required for mitochondrial localisation, while the N teminus is necessary for mitochondrial fission.
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Synonyms
TTC11, Tetratricopeptide repeat domain 11, Fission 1 (mitochondrial outer membrane) homolog (S. cerevisiae).
-
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 MEAVLNELVS VEDLLKFEKK FQSEKAAGSV SKSTQFEYAW CLVRSKYNDD IRKGIVLLEE LLPKGSKEEQ RDYVFYLAVG NYRLKEYEKA LKYVRGLLQT EPQNNQAKEL ERLIDKAMKK DG.
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 :
NME4 Human, ActiveDescription:
Non-Metastatic Cells 4 Human Recombinant, BioActive
Nucleoside diphosphate kinase mitochondrial, Nucleoside diphosphate kinase, mitochondrial, NDK, NDPKD, nm23-H4, NM23D.
Product # :
PRO-2642Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NME4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids (33-187a.a.) and having a molecular mass of 19.6kDa.NME4 is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The NME4 solution (0.5mg/ml) contains 40% glycerol, 20mM Tris-HCl buffer (pH 8.0) and 0.2M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 120unit/mg, and is defined as the amount of enzyme that convert 1.0 umole each of ATP and TDP to ADP and TTP per minute at pH 7.5 at 25C in a couple system with PK/LDH.
More Info
-
Introduction
Non-Metastatic Cells 4 or NME4, is a nucleoside diphosphate kinase located in the mitochondria, and is part of the NDK family of proteins. NME4 ais a very common enzyme that enhances transfer of gamma-phosphates, through a phosphohistidine as a intermediate, between dioxynucleoside tri- and diphosphates. NME4 is originated from the nm23 gene. NME4 has a crucial part in the creation of nucleoside triphosphates that are not ATP.
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Synonyms
Nucleoside diphosphate kinase mitochondrial, Nucleoside diphosphate kinase, mitochondrial, NDK, NDPKD, nm23-H4, NM23D.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPSWTRERTL VAVKPDGVQR RLVGDVIQRF ERRGFTLVGM KMLQAPESVL AEHYQDLRRK PFYPALIRYM SSGPVVAMVW EGYNVVRASR AMIGHTDSAE AAPGTIRGDF SVHISRNVIH ASDSVEGAQR EIQLWFQSSE LVSWADGGQH SSIHPA
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 :
PRDX3 AntibodyDescription:
Peroxiredoxin-3, Mouse Anti Human
AOP1, MER5, AOP-1, SP-22, PRO1748, MGC24293, MGC104387, PRDX3, Thioredoxin-dependent peroxide reductase mitochondrial, Peroxiredoxin-3, PRX III, Antioxidant protein 1, Protein MER5 homolog, HBC189.
Product # :
ANT-630Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
-
Introduction
PRDX3 is part of the peroxiredoxin family of antioxidant enzymes, that reduces hydrogen peroxide and alkyl hydroperoxides. PRDX3 is particularly located in the mitochondria and involved in the regulation of cellular redox status by serving as a primary line of defense against H2O2 produced during respiration. PRDX3 is a significant regulator of the abundance of mitochondrial H(2)O(2), which itself promotes apoptosis in cooperation with other mediators of apoptotic signaling. PRDX3 mitochondrial protein is significantly decreased in Alzheimer Disease and Down Syndrome.
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Synonyms
AOP1, MER5, AOP-1, SP-22, PRO1748, MGC24293, MGC104387, PRDX3, Thioredoxin-dependent peroxide reductase mitochondrial, Peroxiredoxin-3, PRX III, Antioxidant protein 1, Protein MER5 homolog, HBC189.
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Physical Appearance
Sterile filtered colorless solution.
-
Immunogen
Anti-human PRDX3 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human PRDX3 protein 63-256 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG3 heavy chain and k light chain.
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Clone
PAT1F8AT.
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Applications
The antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
-
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.
-
Purification Method
PRDX3 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.
- View Data Sheet
Name :
STAR HumanDescription:
Steroidogenic Acute Regulatory Protein Human Recombinant
Steroidogenic acute regulatory protein, STARD1, StAR, START domain-containing protein 1, cholesterol trafficker, Mitochondrial steroid acute regulatory protein, StAR-related lipid transfer (START) domain containing 1.
Product # :
PRO-979Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
STAR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 243 amino acids (64-285) and having a molecular mass of 27.1 kDa.STAR is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The STAR solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
STAR facilitates the fast increase in pregnenolone synthesis stimulated by tropic hormones. STAR increases pregnenolone synthesis more than four-fold and a major STAR transcription of 1.6 kb is observed in ovary and testis. Throughout the growth and differentiation period of the ovary follicle, the immunoreactivity is likely to move from the granulosa cells of early antral follicles to the theca cell layers in the adult.
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Synonyms
Steroidogenic acute regulatory protein, STARD1, StAR, START domain-containing protein 1, cholesterol trafficker, Mitochondrial steroid acute regulatory protein, StAR-related lipid transfer (START) domain containing 1.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEETLYSDQE LAYLQQGEEA MQKALGILSN QEGWKKESQQ DNGDKVMSKV VPDVGKVFRL EVVVDQPMER LYEELVERME AMGEWNPNVK EIKVLQKIGK DTFITHELAA EAAGNLVGPR DFVSVRCAKR RGSTCVLAGM ATDFGNMPEQ KGVIRAEHGP TCMVLHPLAG SPSKTKLTWL LSIDLKGWLP KSIINQVLSQ TQVDFANHLR KRLESHPASE ARC
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 :
PDHX HumanDescription:
Pyruvate Dehydrogenase Complex, Component X Human Recombinant
DLDBP, E3BP, OPDX, PDX1, proX, Pyruvate Dehydrogenase Complex, Component X, Dihydrolipoamide Dehydrogenase-Binding Protein Of Pyruvate Dehydrogenase Complex, Lipoyl-Containing Pyruvate Dehydrogenase Complex Component X, Pyruvate Dehydrogenase Complex, Lipoyl-Containing Component X, Pyruvate Dehydrogenase Complex, E3-Binding Protein Subunit, Pyruvate Dehydrogenase Protein X Component, Mitochondrial, E3-Binding Protein.
Product # :
ENZ-843Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PDHX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 471 amino acids (54-501 a.a) and having a molecular mass of 50.4kDa. PDHX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PDHX protein solution (0.25mg/ml) containing Phosphate buffer saline (pH 7.4) and 20% glycerol, 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Pyruvate Dehydrogenase Complex, Component X, also known as PDHX, encodes the E3 binding protein subunit of the PDH complex which contains 3 catalytic subunits. PDHX tethers E3 dimers to the E2 core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is critical for a functional PDH complex.
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Synonyms
DLDBP, E3BP, OPDX, PDX1, proX, Pyruvate Dehydrogenase Complex, Component X, Dihydrolipoamide Dehydrogenase-Binding Protein Of Pyruvate Dehydrogenase Complex, Lipoyl-Containing Pyruvate Dehydrogenase Complex Component X, Pyruvate Dehydrogenase Complex, Lipoyl-Containing Component X, Pyruvate Dehydrogenase Complex, E3-Binding Protein Subunit, Pyruvate Dehydrogenase Protein X Component, Mitochondrial, E3-Binding Protein.
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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 MGSGDPIKIL MPSLSPTMEE GNIVKWLKKE GEAVSAGDAL CEIETDKAVV TLDASDDGIL AKIVVEEGSK NIRLGSLIGL IVEEGEDWKH VEIPKDVGPP PPVSKPSEPR PSPEPQISIP VKKEHIPGTL RFRLSPAARN ILEKHSLDAS QGTATGPRGI FTKEDALKLV QLKQTGKITE SRPTPAPTAT PTAPSPLQAT AGPSYPRPVI PPVSTPGQPN AVGTFTEIPA SNIRRVIAKR LTESKSTVPH AYATADCDLG AVLKVRQDLV KDDIKVSVND FIIKAAAVTL KQMPDVNVSW DGEGPKQLPF IDISVAVATD KGLLTPIIKD AAAKGIQEIA DSVKALSKKA RDGKLLPEEY QGGSFSISNL GMFGIDEFTA VINPPQACIL AVGRFRPVLK LTEDEEGNAK LQQRQLITVT MSSDSRVVDD ELATRFLKSF KANLENPIRL A.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TXN2 AntibodyDescription:
Thioredoxin-2, Mouse Anti Human
Thioredoxin mitochondrial, Thioredoxin-2, TXN2, MTRX, TRX2, MT-TRX, TRX-2, TXN-2.
Product # :
ANT-674Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- formulation
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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
Thioredoxin-2 is a low molecular weight redox protein. TRX2 contains a redox active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The TXN2 is involved in the regulation of the mitochondrial membrane potential and in protection against oxidant-induced apoptosis. Upon stimulation of Fas, TXN2 mediates denitrosylation of mitochondria-associated caspase-3, a process required for caspase-3 activation, and promoted apoptosis.
TRX2 is important at low oxidative stress conditions.
MTRX is involved in the regulation of the mitochondrial membrane potential and cell death. Mitochondrial thioredoxin plays an important roles in protection against oxidant-induced apoptosis. Thioredoxin1 and thioredoxin2 have opposed regulatory functions on hypoxia-inducible factor-1alpha. -
Synonyms
Thioredoxin mitochondrial, Thioredoxin-2, TXN2, MTRX, TRX2, MT-TRX, TRX-2, TXN-2.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human TXN2 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human TXN2 protein 60-166 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
PAT1B1AT.
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Applications
The antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
TXN2 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 :
Leptin PufferfishDescription:
Leptin Pufferfish Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-530Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
- source
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Description
Leptin Pufferfish (Takifugu rubripes) Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 16 kDa. Bioactive Leptin Pufferfish (Takifugu rubripes) Recombinant was prepared according to the sequence published by Kurokawa et al. (2005)Peptides 26, 745-750 in two forms: monomer and covalent dimer. MS analysis revealed molecular masses of 15,291 and 30,585 Da, close to the theoretical values of 15,270 and 30,540 Da. CD spectra revealed high similarity to mammalian leptins. Other details of its preparation will be soon published by Yacobovitz et al (in press), General and Comparative Endocrinology.The Pufferfish Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Pufferfish Leptin was lyophilized from a concentrated (0.85mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. The affinity of human leptin receptors is considerably lower campared to mammalian leptins.More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Pufferfish Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Pufferfish Leptin in sterile 0.4% NaHCO3 pH-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
ALPGALDAMDVEKMKSKVTWKAQGLVARIDKHFPDRGLRFDTDKVE
GSTSVVASLESYNNLISDRFGGVSQIKTEISSLAGYLNHWREGNCQE
QQPKVWPRRNIFNHTVSLEALMRVREFLKLLQKNVDLLERC
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 1.28 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 :
ALDH2 MouseDescription:
Aldehyde Dehydrogenase 2 Mouse Recombinant
Aldehyde dehydrogenase, mitochondrial, AHD-M1, ALDH class 2, ALDH-E2, ALDHI.
Product # :
ENZ-879Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ALDH2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 523 amino acids (20-519 a.a) and having a molecular mass of 56.8kDa. ALDH2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ALDH2 protein e solution (0.5mg/ml) containing Phosphate buffered salin(pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
ALDH2 is part of the aldehyde dehydrogenase family of proteins which catalyze the chemical transformation from acetaldehyde to acetic acid. ALDH2 is the second enzyme of the major oxidative pathway of alcohol metabolism. ALDH2 has 2 major liver isoforms: cytosolic and mitochondrial, which differ by their electrophoretic mobilities, kinetic properties, and subcellular localizations. Nearly all Caucasians have 2 major isozymes, whereas roughly 50% of Orientals have only the cytosolic isozyme, omitting the mitochondrial isozyme. The extremely higher rate of acute alcohol intoxication with Orientals compared to Caucasians is due to the fact of the absence of mitochondrial isozyme. ALDH2 has a low Km for acetaldehydes, and is localized in mitochondrial matrix.
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Synonyms
Aldehyde dehydrogenase, mitochondrial, AHD-M1, ALDH class 2, ALDH-E2, ALDHI.
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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 MGSSAAATSA VPAPNHQPEV FCNQIFINNE WHDAVSRKTF PTVNPSTGEV ICQVAEGNKE DVDKAVKAAR AAFQLGSPWR RMDASDRGRL LYRLADLIER DRTYLAALET LDNGKPYVIS YLVDLDMVLK CLRYYAGWAD KYHGKTIPID GDFFSYTRHE PVGVCGQIIP WNFPLLMQAW KLGPALATGN VVVMKVAEQT PLTALYVANL IKEAGFPPGV VNIVPGFGPT AGAAIASHEG VDKVAFTGST EVGHLIQVAA GSSNLKRVTL ELGGKSPNII MSDADMDWAV EQAHFALFFN QGQCCCAGSR TFVQENVYDE FVERSVARAK SRVVGNPFDS RTEQGPQVDE TQFKKILGYI KSGQQEGAKL LCGGGAAADR GYFIQPTVFG DVKDGMTIAK EEIFGPVMQI LKFKTIEEVV GRANDSKYGL AAAVFTKDLD KANYLSQALQ AGTVWINCYD VFGAQSPFGG YKMSGSGREL GEYGLQAYTE VKTVTVKVPQ KNS.
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 :
AK2 HumanDescription:
Adenylate Kinase 2 Human Recombinant
ADK2, AK-2, Adenylate kinase isoenzyme 2 mitochondrial, ATP-AMP transphosphorylase 2, adenylate kinase 2.
Product # :
PKA-260Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
AK2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 259 amino acids and having a molecular mass of 28.6 kDa. AK2 is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AK2 solution containing 20mM Tris pH-7.5, 5mM DTT and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity: > 1.5 units/ml. One unit will convert 2.0 umoles of ADP to ATP + AMP per minute at pH 7.5 at 25C.More Info
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Introduction
Adenylate kinases play a role in regulating the adenine nucleotide composition within a cell by catalyzing the reversible transfer of phosphate groups among adenine nucleotides. There are 3 types of adenylate kinase isozymes, AK1, AK2, and AK3 in vertebrates. Expression of these isozymes are tissue-specific and developmentally regulated. AK2 is localized in the mitochondrial intermembrane space and is involved in apoptosis. AK2 is mutated in individuals with reticular dysgenesis.
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Synonyms
ADK2, AK-2, Adenylate kinase isoenzyme 2 mitochondrial, ATP-AMP transphosphorylase 2, adenylate kinase 2.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
AK2 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAPSVPAAEP EYPKGIRAVL LGPPGAGKGTQAPRLAENFC VCHLATGDML RAMVASGSEL GKKLKATMDA GKLVSDEMVV ELIEKNLETP LCKNGFLLDG FPRTVRQAEM LDDLMEKRKE KLDSVIEFSIPDSLLIRRIT GRLIHPKSGR SYHEEFNPPK EPMKDDITGE PLIRRSDDNE KALKIRLQAY HTQTTPLIEY YRKRGIHSAI DASQTPDVVF ASILAAFSKA TCKDLVMFI.
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 :
DLD HumanDescription:
Dihydrolipoamide Dehydrogenase Human Recombinant
EC 1.8.1.4, DLD, DLDH, GCSL, PHE3, Dihydrolipoyl dehydrogenase mitochondrial, Dihydrolipoamide dehydrogenase, Glycine cleavage system L protein, LAD, E3.
Product # :
ENZ-502Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DLD Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 511 amino acids (36-509 a.a.) and having a molecular mass of 54.4 kDa. The DLD is fused to a 37 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DLD solution contains 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
DLD is an L protein of the mitochondrial glycine cleavage system which is also a component of the pyruvate dehydrogenase complex, the alpha-ketoglutarate dehydrogenase complex, and the branched-chain alpha-keto acide dehydrogenase complex. DLD mutations were found in patients with E3-deficient maple syrup urine disease and lipoamide dehydrogenase deficiency.
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Synonyms
EC 1.8.1.4, DLD, DLDH, GCSL, PHE3, Dihydrolipoyl dehydrogenase mitochondrial, Dihydrolipoamide dehydrogenase, Glycine cleavage system L protein, LAD, E3.
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Physical Appearance
Sterile Filtered clear colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMADQ PIDADVTVIG SGPGGYVAAI KAAQLGFKTV CIEKNETLGG TCLNVGCIPS KALLNNSHYY HMAHGKDFAS RGIEMSEVRL NLDKMMEQKS TAVKALTGGI AHLFKQNKVV HVNGYGKITG KNQVTATKAD GGTQVIDTKN ILIATGSEVT PFPGITIDED TIVSSTGALS LKKVPEKMVV IGAGVIGVEL GSVWQRLGAD VTAVEFLGHV GGVGIDMEIS KNFQRILQKQ GFKFKLNTKV TGATKKSDGK IDVSIEAASG GKAEVITCDV LLVCIGRRPF TKNLGLEELG IELDPRGRIP VNTRFQTKIP NIYAIGDVVA GPMLAHKAED EGIICVEGMA GGAVHIDYNC VPSVIYTHPE VAWVGKSEEQ LKEEGIEYKV GKFPFAANSR AKTNADTDGM VKILGQKSTD RVLGAHILGP GAGEMVNEAA LALEYGASCE DIARVCHAHP TLSEAFREAN LAASFGKSIN F.
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.