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1000 results found for “secreted frizzled-related protein”
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Name :
Desmin ChickenDescription:
Desmin Chicken Gizzard
Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.
Product # :
PRO-2783Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Desmin Chicken having a calculated molecular mass of 53 kDa, pI-5.4.
Source
Chicken gizzard.
Formulation
Desmin was lyophilized from a 1mg/ml solution containing 10 mM sodium phosphate buffer pH 7.5, 6M urea, 1mM EDTA, 2mM DTT and 10mM methylammonium chloride.
Purity
Greater than 98.0% as determined by SDS-PAGE.
Citations
More Info
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Synonyms
Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized Desmin between 2-8°C, do not freeze. Upon reconstitution Desmin should be stored at -20°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Desmin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
Desmin, an intermediate filament protein, plays a fundamental role in maintaining the structural integrity and function of muscle cells. While extensive research has been conducted on desmin in mammals, the study of desmin in chickens is an emerging area with considerable potential for advancing our understanding of muscle biology. Chickens are valuable model organisms for studying muscle development, growth, and regeneration due to their relatively simple muscular system and economic significance in poultry production. This research aims to provide a comprehensive exploration of desmin in chickens, shedding light on its functions and implications for muscle structure and function.
The primary objective of this research is to elucidate the role of desmin in chicken muscle structure and development. In vitro and in vivo experiments, utilizing chicken cell cultures and embryonic models, will be conducted to investigate how desmin contributes to the organization of muscle fibers, sarcomere assembly, and myofibrillogenesis. Understanding these mechanisms is fundamental for deciphering the complexities of muscle development in chickens.
The second objective is to assess the clinical and economic relevance of desmin in poultry production. Studies involving broiler chickens will be conducted to evaluate the impact of desmin mutations or variations on muscle growth, meat quality, and disease susceptibility. These investigations may provide valuable insights into potential strategies for enhancing poultry production efficiency and meat quality.
The third objective is to explore the potential applications of desmin in biotechnology and tissue engineering. Research will investigate the use of desmin-expressing chicken cells as models for studying muscle-related diseases and for developing tissue engineering approaches for muscle repair and regeneration.
By delving into the functions and roles of desmin in chickens, this research aims to expand our knowledge of muscle biology, its implications for poultry production, and its potential applications in biotechnology and regenerative medicine.
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 :
SPA 33.4kDaDescription:
Staphylococcal Protein-A 33.4kDa Recombinant
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
Product # :
PRO-1921Price :
Quantity :
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Shipped at Room temp
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Description
SPA Recombinant produced in E.Coli is a homodimeric non-glycosylated polypeptide chains comprised of 5 IgG-binding domains E-D-A-B-C aligned in series containing 296 amino acids and having a molecular mass of 33.4kDa containing little or no carbohydrate. Cell wall binding region, cell membrane binding region and albumin binding region were removed to ensure the highest specific IgG binding.
Source
Escherichia Coli.
Formulation
SPA protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by: (a) Analysis by HPLC.(b) Analysis by SDS-PAGE.
Citations
More Info
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Introduction
Protein A is a cell wall component produced by several strains of Staphylococcus aureus. The recombinant Protein A is genetically engineered protein and holds 5 IgG-binding regions of protein A. Recombinant Protein A functions basically the same as native Protein A and is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to human IgG1, IgG2 and IgG4, mouse IgG2a, IgG2b and IgG3 and rat IgG2c. Protein A also binds to total IgG from rabbit, pig, dog, cat, and guinea pig.
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Synonyms
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SPA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SPA 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 SPA in sterile 18MΩ-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEED.
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 :
CRYGS HumanDescription:
Crystallin, Gamma S Human Recombinant
Crystallin gamma S, Gamma-crystallin S, CRYG8, crystallin, gamma 8, Beta-crystallin S.
Product # :
PRO-963Price :
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Shipped with Ice Packs
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Description
CRYGS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 202 amino acids (1-178) and having a molecular mass of 23.6 kDa.The CRYGS is fused to a 24 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CRYGS solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Mammalian crystallins which are water soluble structural proteins located in the vertebrate eye are classified in three forms, labeled alpha, beta and gamma. Crystallins, the primary components of the lens, raise the refractive index of the eye all through the accommodation by creating high-molecular weight aggregates that maintain transparency. CRYGS is a monomer that does not aggregate. CRYGS encodes the most substantial gamma-crystallin in adult eye lens tissue. Gamma-crystallins has a part in cataract formation due to aging or mutations in specific genes,
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Synonyms
Crystallin gamma S, Gamma-crystallin S, CRYG8, crystallin, gamma 8, Beta-crystallin S.
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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 MGSHMSKTGT KITFYEDKNF QGRRYDCDCD CADFHTYLSR CNSIKVEGGT WAVYERPNFA GYMYILPQGE YPEYQRWMGL NDRLSSCRAV HLPSGGQYKI QIFEKGDFSG QMYETTEDCP SIMEQFHMRE IHSCKVLEGV WIFYELPNYR GRQYLLDKKE YRKPIDWGAA SPAVQSFRRI VE
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 :
FLRT3 HumanDescription:
Fibronectin Leucine Rich Transmembrane Protein 3 Human Recombinant
Fibronectin Leucine Rich Transmembrane Protein 3, Fibronectin-Like Domain, Containing Leucine-Rich Transmembrane Protein 3, HH21, Leucine-Rich Repeat, Transmembrane Protein FLRT3, KIAA1469.
Product # :
PRO-2181Price :
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Shipped with Ice Packs
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Description
FLRT3 produced in Sf9 insect cells is a single, glycosylated polypeptide chain containing 508 amino acids (29-528a.a.) and having a molecular mass of 57.6kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).FLRT3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
FLRT3 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Fibronectin Leucine Rich Transmembrane Protein 3, also known as FLRT3 is a member of the fibronectin leucine rich transmembrane protein (FLRT) family. FLRT3 contains one fibronectin type-III domain as well as 10 LRR (leucine-rich) repeats and is expressed in the kidney, brain, pancreas, skeletal muscle, lung, liver, placenta, and heart. In addition, the members of the FLRT family play a role in cell adhesion as well as receptor signaling. FLRT3 has been implicated in neurite outgrowth after nerve damage, as a positive regulator of FGF signalling and in homotypic cell adhesion. Furthermore, FLRT3 has an essential function in regulating cellular adhesion among the epithelial apical ridge and the underlying mesenchyme and also in the establishment of the dorso-ventral position of the ridge.
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Synonyms
Fibronectin Leucine Rich Transmembrane Protein 3, Fibronectin-Like Domain, Containing Leucine-Rich Transmembrane Protein 3, HH21, Leucine-Rich Repeat, Transmembrane Protein FLRT3, KIAA1469.
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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
KSCPSVCRCD AGFIYCNDRF LTSIPTGIPE DATTLYLQNN QINNAGIPSD LKNLLKVERI YLYHNSLDEF PTNLPKYVKE LHLQENNIRT ITYDSLSKIP YLEELHLDDN SVSAVSIEEG AFRDSNYLRL LFLSRNHLST IPWGLPRTIE ELRLDDNRIS TISSPSLQGL TSLKRLVLDG NLLNNHGLGD KVFFNLVNLT ELSLVRNSLT AAPVNLPGTN LRKLYLQDNH INRVPPNAFS YLRQLYRLDM SNNNLSNLPQ GIFDDLDNIT QLILRNNPWY CGCKMKWVRD WLQSLPVKVN VRGLMCQAPE KVRGMAIKDL NAELFDCKDS GIVSTIQITT AIPNTVYPAQ GQWPAPVTKQ PDIKNPKLTK DHQTTGSPSR KTITITVKSV TSDTIHISWK LALPMTALRL SWLKLGHSPA FGSITETIVT GERSEYLVTA LEPDSPYKVC MVPMETSNLY LFDETPVCIE TETAPLRMYN PTTTLNREQE KEPYKNPNLP LEHHHHHH.
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 :
SPINK1 HumanDescription:
Serine Peptidase Inhibitor Kazal Type 1 Human Recombinant
Serine Peptidase Inhibitor Kazal Type 1, Pancreatic Secretory Trypsin Inhibitor, Tumor-Associated Trypsin Inhibitor, PCTT, TATI, Spink3, Serine Protease Inhibitor Kazal Type 1, TCP, PSTI.
Product # :
ENZ-724Price :
Quantity :
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Shipped with Ice Packs
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Description
SPINK1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 79 amino acids (24-79) and having a molecular mass of 8.6kDa.SPINK1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SPINK1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Trypsin inhibitor SPINK1 is secreted from pancreatic acinar cells into pancreatic fluid. SPINK1 has a role in inhibition of trypsin-catalyzed premature initiation of zymogens in the pancreas and the pancreatic duct. Alterations in SPINK1 gene are the cause for tropical calcific and pancreatitis hereditary pancreatitis.
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Synonyms
Serine Peptidase Inhibitor Kazal Type 1, Pancreatic Secretory Trypsin Inhibitor, Tumor-Associated Trypsin Inhibitor, PCTT, TATI, Spink3, Serine Protease Inhibitor Kazal Type 1, TCP, PSTI.
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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 MGSDSLGREA KCYNELNGCT KIYDPVCGTD GNTYPNECVL CFENRKRQTS ILIQKSGPC.
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 :
MUC16 HumanDescription:
Mucin-16 (CA125) Human
Product # :
PRO-2746Price :
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Description
The Human Mucin-16 (CA125) was purified from Human carcinoma cell line.
Source
Human carcinoma cell line.
Formulation
MUC16 is supplied in a 0.05M sodium phosphate buffer, pH 7.5, 0.09% NaN3 and 0.15M NaCl.
Purity
Greater than 60%.
Citations
More Info
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Introduction
MUC16, aka CA125, is a mucin protein that might be found in type I transmembrane or secreted forms that are used monitor the progress of epithelial ovarian cancer therapy.
The CA125 molecule is heterogeneous with regard to both size and charge, almost certainly due to continuous deglycosylation of side chains during its life-span in bodily fluids.
MUC16 is most likely a glycoprotein with a predominance of O-linkages. -
Physical Appearance
Clear colorless to pale blue frozen solution.
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Stability
Human MUC16 although stable at 4°C for 1 week, should be stored at -20°C.
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Human Virus Test
Tissue sample tested and found negative for HIV-1 & 2 antibodies, HBsAg, and Hepatitis-C antibodies.
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 :
CRYAB Human, HisDescription:
Crystallin Alpha B Human Recombinant, His Tag
CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.
Product # :
HSP-088Price :
Quantity :
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Shipped with Ice Packs
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Description
CRYAB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (1-175) and having a molecular mass of 21.2kDa. CRYAB is fused to an 8 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CRYAB solution (1mg/ml) contains 10% glycerol & Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Synonyms
CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.
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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
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSW FDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVT AAPKKLEHHH HHH.
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Background
Alpha-B crystallin (CRYAB), a small heat shock protein, stands as a multifaceted molecular chaperone integral to cellular homeostasis and stress response. In its human recombinant form, CRYAB becomes a focal point in biomedical research, offering a controlled platform to explore its structural intricacies, cellular functions, and potential therapeutic applications. This research embarks on a comprehensive journey to unveil the diverse roles of CRYAB Human Recombinant, shedding light on its structural attributes, cellular interactions, and its implications in health and disease. By delving into the properties of CRYAB, scientists aim to deepen our understanding of cellular proteostasis and explore novel avenues in the treatment of protein misfolding disorders.
Structural Insights into CRYAB Human Recombinant:
CRYAB, forming oligomeric complexes, possesses a dynamic structural configuration crucial for its chaperone function. The human recombinant form, designed for controlled study, provides a unique window into the three-dimensional intricacies of CRYAB. Understanding its structure is fundamental for deciphering how CRYAB engages with client proteins, preventing their aggregation and maintaining cellular proteostasis.
Cellular Functions in Proteostasis:
As a molecular chaperone, CRYAB plays a pivotal role in preserving cellular proteostasis by preventing the aggregation of misfolded proteins. Beyond its chaperone function, CRYAB is implicated in diverse cellular processes, including modulation of apoptosis, regulation of cytoskeletal dynamics, and participation in cell signaling pathways. Elucidating the multifaceted functions of CRYAB Human Recombinant provides insights into its roles in health and disease.
Implications in Neurodegenerative Disorders:
CRYAB has garnered attention in the context of neurodegenerative disorders, where protein misfolding and aggregation are central pathological features. Studies involving CRYAB Human Recombinant have revealed its neuroprotective properties, suggesting its potential as a therapeutic target for conditions like Alzheimer's and Parkinson's diseases. Understanding the mechanisms by which CRYAB mitigates protein aggregation in neuronal cells holds promise for developing targeted interventions.
CRYAB in Cardiovascular Health:
The chaperone function of CRYAB extends to the cardiovascular system, where it safeguards against protein aggregation in cardiomyocytes. CRYAB Human Recombinant studies have illuminated its protective role in cardiac tissues, positioning it as a potential therapeutic avenue for heart diseases characterized by protein misfolding.
Challenges and Future Directions:
While the potential of CRYAB Human Recombinant in therapeutics is evident, challenges persist. Fine-tuning its applications, understanding its interactions with diverse client proteins, and exploring the intricacies of its roles in different cellular contexts are critical for translational success. Additionally, deciphering the specific mechanisms by which CRYAB contributes to the alleviation of protein misfolding disorders remains an active area of investigation.
CRYAB Human Recombinant emerges as a linchpin in the cellular orchestra, orchestrating a symphony of functions vital for proteostasis. Its structural insights, diverse cellular functions, and therapeutic implications position it at the forefront of biomedical research. As researchers continue to unravel the molecular nuances of CRYAB, they not only deepen our understanding of cellular proteostasis but also pave the way for innovative treatments in neurodegenerative and cardiovascular disorders, shaping the future of precision medicine and protein folding therapeutics.
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 :
Gliadin Alpha WheatDescription:
Gliadin Alpha Wheat Recombinant
Product # :
PRO-2147Price :
Quantity :
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Description
Recombinant Wheat Gliadin Alpha protein produced in E.Coli and fused to a 6 His Tag at C-terminus, having a theoretical Mw of 34557.64 Dalton, pI 7.70. Purified by proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
Gliadin Alpha protein solution in 10mM Tris-HCl pH 7.2.
Purity
Protein is >90% pure.
Citations
More Info
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Introduction
Wheat Gliadin and related gluten components from barley, rye and possibly oats can cause an abnormal immune response called Celiac disease which is a chronic gastrointestinal disorder. Celiac disease characteristics are flattening of the jejunal mucosa and intestinal lesions of variable severity in hereditarily inclined individuals. Even though Celiac disease is not a classic autoimmune disease it is related to anti-tissue transglutaminase antibodies and gliadin antibodies tests are most recommended in screening populations at risk for CD and other gluten-sensitive enteropathies. In the past, serologic tests for gliadin antibodies usually were not very precise and were not enough for accurate diagnosis due to missing deamidated epitopes within the authentic gliadin fraction traditionally used in diagnostic test kits. ProSpec's deamidated Gliadin isoform matches to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Gliadin Alpha 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
MVRVPVPQLQPQNPSQQQPQEQVPLVQQQQFPGQQQPFPPQQPYPQPQPFPSQQPYLQ
LQPFPQPQLPYPQPQLPYPQPQLPYPQPQPFRPQQPYPQSQPQYSQPQQPISQQQQQQQQ
QQQQKQQQQQQQQILQQILQQQLIPCRDVVLQQHSIAYGSSQVLQQSTYQLVQQLCCQQL
WQIPEQSRCQAIHNVVHAIILHQQQQQQQQQQQQPLSQVSFQQPQQQYPSGQGSFQPSQ
QNPQAQGSVQPQQLPQFEEIRNLALETLPAMCNVYIPPYCTIAPVGIFGTNYRHHHHHH.
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 :
MAPT Human 381a.a.Description:
Microtubule-Associated Protein Tau 381 a.a. Human Recombinant
Microtubule-associated protein tau, isoform CRA_f, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.
Product # :
PRO-042Price :
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Shipped with Ice Packs
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Description
MAPT 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 401 amino acids (1-381 a.a.) and having a molecular mass of 41.8kDa. The NCBI Accession No. is EAW93573.1.The MAPT is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MAPT solution (0.5 mg/ml) contains 20mM Tris-HCl Buffer (pH 7.5), 1mM DTT and 20% Glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Microtubule-associated protein tau (MAPT or Tau) is a protein that stabilizes microtubules. MAPT is abundant in neurons in the central nervous system and is less common elsewhere. When MAPT is defective, and no longer stabilizes microtubules properly, it can result in dementias, such as Alzheimer's disease.
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Synonyms
Microtubule-associated protein tau, isoform CRA_f, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.
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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 MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKESPLQT PTEDGSEEPG SETSDAKSTP TAEAEEAGIG DTPSLEDEAA GHVTQARMVS KSKDGTGSDD KKAKGADGKT KIATPRGAAP PGQKGQANAT RIPAKTPPAP KTPPSSGEPP KSGDRSGYSS PGSPGTPGSR SRTPSLPTPP TREPKKVAVV RTPPKSPSSA KSRLQTAPVP MPDLKNVKSK IGSTENLKHQ PGGGKVQIVY
KPVDLSKVTS KCGSLGNIHH KPGGGQVEVK SEKLDFKDRV QSKIGSLDNI THVPGGGNKK IETHKLTFRE NAKAKTDHGA EIVYKSPVVS GDTSPRHLSN VSSTGSIDMV DSPQLATLAD EVSASLAKQG L.
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 :
Protein A/GDescription:
Protein A/G Recombinant
Product # :
PRO-646Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The recombinant Protein A/G consists of 5 IgG-binding regions of protein A and 2 of protein G, which corresponds to the Protein A and G domains that are included in the recombinant sequence. Cell wall binding region, cell membrane binding region and albumin binding region have been removed from the recombinant Protein A/G to ensure the maximum specific IgG binding. The Protein A portion is from Staphylococcus aureus segments E, D, A, B and C. The Protein G portion is from Streptococcus segments C1 and C3. The fusion protein has a predicted molecular mass of 47.7kDa and containing 429 amino acids.
Source
Escherichia coli.
Formulation
Lyophilized white Powder containing no additives.
Purity
>97% as determined by SDS-PAGE and RP-HPLC.
Citations
More Info
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Introduction
Recombinant Protein A/G fusion protein joins IgG binding domains of both Protein A and Protein G.
Protein A/G includes four Fc binding domains from Protein A and two from Protein G, yielding a final mass of 50.4 kDa. The binding dependency to pH of Protein A/G lower than Protein A, but has the additive properties of Protein A and G together. Protein A/G binds to all subclasses of human IgG, making it helpful for purifying polyclonal or monoclonal IgG antibodies whose subclasses have not been identifieed. Protein A/G binds to IgA, IgE, IgM and IgD. Protein A/G binds to all subclasses of mouse IgG excluding mouse IgA, IgM or serum albumin. This permits Protein A/G to be used in purification and detection of mouse monoclonal IgG antibodies, with no interference from IgA, IgM and serum albumin. Mouse monoclonal antibodies normally have a stronger affinity to the chimeric Protein A/G than to either Protein A or Protein G. Protein A/G also has been used for purification of macaque IgG. -
Stability
After reconstitution, aliquot and store at -20°C. Avoid repeated freeze/thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Protein-A/G in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDSLEG SGSGTYKLIL NGKTLKGETT TEAVDAATAE KVFKQYANDN GVDGEWTYDD ATKTFTVTEK PEVIDASELT PAVTTYKLVI NGKTLKGETT TKAVDAETAE KAFKQYANDN GVDGVWTYDD ATKTFTVTE.
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 :
GlycininDescription:
Allergen Ara h 3.0101 Recombinant
Glycinin, Arah3.
Product # :
ALR-008Price :
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Description
Recombinant Glycinin produced in E. coli is a non- glycosylated, polypeptide chain having a calculated molecular mass of 63 kDa. Glycinin is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Glycinin is supplied in 20mM HEPES buffer pH-8, 6M Urea and 0.25M NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Glycinin Ara h 3 is a seed storage protein, 11 S globulin and trypsin inhibitor from peanut. Each subunit of the hexamer is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond. Ara h 3 and Ara h 4 are isoforms. Glycinin is the source of sulfur-containing amino acids in seed meals and it exists in the seeds of many leguminous and non-leguminous plants.
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Synonyms
Glycinin, Arah3.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SEC61B HumanDescription:
SEC61B Human Recombinant
Protein transport protein Sec61 subunit beta, SEC61B, Sec61 Beta Subunit, Protein Translocation Complex Beta, Protein Transport Protein SEC61 Beta Subunit, Sec61 Complex Beta Subunit.
Product # :
PRO-1795Price :
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Description
SEC61B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids (1-70 a.a) and having a molecular mass of 9.4kDa.SEC61B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SEC61B protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
The Sec61 complex is the key component of the protein translocation apparatus of the ER (endoplasmic reticulum) membrane. Oligomers of the Sec61 complex construct a transmembrane channel where proteins are translocated across and incorporated into the ER membrane. This complex consists of 3 membrane proteins- alpha, beta, and gamma. The SEC61B gene encodes the beta-subunit protein. The Sec61 subunits are also detected in the post-ER compartment, suggesting that these proteins can get out of the ER and recycle back.
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Synonyms
Protein transport protein Sec61 subunit beta, SEC61B, Sec61 Beta Subunit, Protein Translocation Complex Beta, Protein Transport Protein SEC61 Beta Subunit, Sec61 Complex Beta Subunit.
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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 MGSMPGPTPS GTNVGSSGRS PSKAVAARAA GSTVRQRKNA SCGTRSAGRT TSAGTGGMWR FYTEDSPGLK VGP.
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 :
LIN28 HumanDescription:
LIN28 Human Recombinant
CSDD1, FLJ12457, LIN-28, LIN28A, Protein lin-28 homolog A, ZCCHC1, Zinc finger CCHC domain-containing protein 1, Lin-28A, LIN28.
Product # :
PRO-743Price :
Quantity :
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Description
Recombinant Human LIN28 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (42-209) and having a molecular mass of 21.1 kDa.LIN28 is expressed with a 23 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LIN28 protein solution (0.5mg/ml) contains 20mM Tris-HCl, pH-8, 10% glycerol, 0.1mM PMSF and 0.1M NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE
Citations
More Info
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Introduction
LIN28 plays an important role as a 'translational enhancer', leading specific mRNAs to polysomes and therefore increasing the competence of protein synthesis. LIN28 is a marker of undifferentiated human embryonic stem cells and it enhances the efficiency of the formation of induced pluripotent stem (iPS) cells from human fibroblasts. LIN28 binds to the let-7 pre-miRNA and blocks production of the mature let-7 microRNA in mouse embryonic stem cells. Overexpression of LIN28 is associated with human germ-cell tumors.
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Synonyms
CSDD1, FLJ12457, LIN-28, LIN28A, Protein lin-28 homolog A, ZCCHC1, Zinc finger CCHC domain-containing protein 1, Lin-28A, LIN28.
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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 SSGLVPRGSHRSMGICKWFN VRMGFGFLSM TARAGVALDP PVDVFVHQSK LHMEGFRSLK EGEAVEFTFK KSAKGLESIR VTGPGGVFCI GSERRPKGKS MQKRRSKGDR CYNCGGLDHH AKECKLPPQP KKCHFCQSIS HMVASCPLKA QQGPSAQGKP TYFREEEEEI HSPTLLPEAQ N.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CRYAB HumanDescription:
Crystallin Alpha B Human Recombinant
CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.
Product # :
HSP-003Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant CRYAB produced in E.Coli is a single,non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 20.1kDa. CRYAB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CRYAB protein (1mg/ml) solution contains 20mM Tris-HCl buffer pH-7.5, 50mM NaCl and 1mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Alpha crystallins are composed of two gene products ; alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20). They act as molecular chaperones and hold them in in large soluble aggregates. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional function of a-crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-B is expressed widely in many tissues and organs and occurs in many neurological diseases.
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Synonyms
CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.
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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
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSWFDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHRKYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVT AAPKK.
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 :
CRISP1 HumanDescription:
Cysteine-Rich Secretory Protein 1 Human Recombinant
Cysteine-rich secretory protein 1, ARP, CRISP-1, AEGL1, Acidic epididymal glycoprotein-like 1, HSCRISP1D, HSCRISP1G, HUMARP, AEG-like protein, cysteine-rich secretory protein-1 delta.
Product # :
PRO-473Price :
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Shipped at Room temp
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Description
The CRISP1 Protein Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 238 amino acids (Lys 22 - Lys 249) having a molecular mass of 27kDa.CRISP1 is fused to 10 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a 0.5mg/ml solution containing 20mM TRIS, 50mM NaCl, pH 7.5.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Insemination involves of a series of specific cell-cell interactions concluding in the fusion of the sperm and egg plasma membranes. Recognition, binding, and fusion take place through the interface of complementary molecules which are localized to specific domains of the sperm and egg plasma membranes. In the sperm, the postacrosomal region or equatorial segment is involved in sperm-egg plasma membrane fusion. The protein encoded by this gene belongs to the cysteine-rich secretory protein (CRISP) family. CRISP1 is expressed in the epididymis, is secreted into the epididymal lumen, and binds to the postacrosomal region of the sperm head, where it takes part in sperm-egg fusion.
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Synonyms
Cysteine-rich secretory protein 1, ARP, CRISP-1, AEGL1, Acidic epididymal glycoprotein-like 1, HSCRISP1D, HSCRISP1G, HUMARP, AEG-like protein, cysteine-rich secretory protein-1 delta.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CRISP1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CRISP1 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 CRISP1 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
MKHHHHHHAS KKKSARDQFN KLVTDLPNVQ EEIVNIHNAL RRRVVPPASN MLKMSWSEEA AQNARIFSKY CDMTESNPLE RRLPNTFCGE NMHMTSYPVS WSSVIGVWYS ESTSFKHGEW TTTDDDITTD HYTQIVWATS YLIGCAIASC RQQGSPRYLY VCHYCHEGND PETKNEPYKT GVPCEACPSN CEDKLCTNPC IYYDEYFDCD IQVHYLGCNH STTILFCKAT CLCDTEIK
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Applications
Western blotting, ELISA.
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 :
RELM b HumanDescription:
RELM-Beta Human Recombinant
Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.
Product # :
CYT-780Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
RELM-b Human Recombinant produced in E.Coli is a disulfide-linked homodimer, non-glycosylated, polypeptide chain containing 2 x 89 amino acids and having a total molecular mass of 19kDa. RELM-b is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RELM-b was lyophilized from a solution containing 0.1% Trifluoroacetic Acid (TFA).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
RELM-beta (Resistin-Like Molecule-beta) is a member of a recently identified family of secreted proteins containing a conserved cystein-rich C-terminus. The RELM family consists of resistin (also called FIZZ3), RELM-alfa (FIZZ1), RELM-beta (FIZZ2) and RELM-gamma. Only resisistin and RELM-beta were found in humans whereas all four RELM family members were identified in rodents.
RELM-beta appears to be produced as a homodimer exclusively by intestinal goblet cells and can be found in high quantities in stool. Remarkably, stool of germ-free mice displaying sterile intestinal tract does not contain RELM-beta until bacterial colonization takes place after pathogen-free mice entered natural environment. Some, but not all, colon carcinoma cell lines secrete RELM-beta into the cell culture supernatant.
The physiological function of RELM-beta is not known. High doses of recombinant RELM-beta showed hyperglycemic effects including lowered glucose disposal and increased hepatic glucose production in mice. -
Synonyms
Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized RELM-b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution RELM-b Human Recombinant 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 RELM-b in sterile 0.1% TFA not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MQCSLDSVMD KKIKDVLNSL EYSPSPISKK LSCASVKSQG RPSSCPAGMA VTGCACGYGC GSWDVQLETT CHCQCSVVDW TTARCCHLT.
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 :
NEFH BovineDescription:
Neurofilament Heavy Chain Bovine
Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.
Product # :
PRO-2787Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
NEFH Bovine having a calculated molecular mass of 200 kDa, pI-5.5.
Source
Bovine spinal cord.
Formulation
NEFH was lyophilized from a 1mg/ml solution containing 10mM sodium phosphate buffer pH 7.5, 6M urea, 1mM EDTA, 2mM DTT and 10mM methylammonium chloride.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Synonyms
Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized NEFH between 2-8°C, do not freeze. Upon reconstitution NEFH should be stored at -20°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized NEFH 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
Neurofilament heavy chain (NEFH) is a vital structural protein in neurons, predominantly found in the central and peripheral nervous systems. Although extensive research has been conducted on NEFH in humans and rodents, the investigation of NEFH in bovine nervous tissues presents an emerging area with substantial potential for advancing our understanding of neuronal biology in larger mammals and its applications in veterinary medicine and neurobiology.
Bovine nervous tissues, including the brain and spinal cord, are of particular interest due to their relevance in cattle health, neuroscience, and the food industry. This research aims to provide a comprehensive exploration of NEFH in bovine nervous tissues, elucidating its functions, structural significance, and potential applications.
The primary objective of this research is to elucidate the role of NEFH in bovine nervous tissues, particularly in maintaining neuronal structural integrity and axonal function. In vitro and ex vivo experiments, utilizing bovine neuronal cell cultures and tissue specimens, will be conducted to investigate how NEFH contributes to neuronal morphology, axonal transport, and overall neuronal resilience. Understanding these mechanisms is fundamental for deciphering the complexities of neuronal biology in bovine species.
The second objective is to assess the relevance of bovine NEFH in veterinary medicine. Studies involving bovine models will be conducted to evaluate the impact of NEFH mutations or variations on neuronal health, disease susceptibility, and neurodegenerative conditions. These investigations may provide valuable insights into potential applications in cattle health, the development of diagnostic tools for neurological disorders, and strategies for enhancing animal welfare.
The third objective is to explore the potential applications of bovine NEFH in neurobiology and biotechnology. Research will investigate the use of bovine NEFH-expressing cells as models for studying neuronal-related diseases and for developing tissue engineering approaches in veterinary medicine and biotechnology.
By delving into the functions and roles of NEFH in bovine nervous tissues, this research aims to expand our knowledge of neuronal biology, its implications for veterinary medicine, and its potential applications in neurobiology, cattle health, and biotechnology.
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 :
LZIC HumanDescription:
Leucine Zipper And CTNNBIP1 Domain Containing Human Recombinant
WAP Four-Disulfide Core Domain 12, Putative Protease Inhibitor WAP12, Whey Acidic Protein 2, Chromosome 20 Open Reading Frame 122, Protease Inhibitor WAP2, Single WAP Motif Protein 2, WAP Four-Disulfide Core Domain Protein 12, dJ211D12.4, C20orf122, SWAM2, WAP2.
Product # :
PRO-1831Price :
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Description
LZIC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 111 amino acids (24-111) and having a molecular mass of 12.1 kDa. LZIC is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The LZIC solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
LZIC is a member of the CTNNBIP1 family. LZIC protein is universally expressed, with largest levels in kidney and up-regulated in various cases of gastric cancers. LZIC has no interaction with CTNNB1.
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Synonyms
WAP Four-Disulfide Core Domain 12, Putative Protease Inhibitor WAP12, Whey Acidic Protein 2, Chromosome 20 Open Reading Frame 122, Protease Inhibitor WAP2, Single WAP Motif Protein 2, WAP Four-Disulfide Core Domain Protein 12, dJ211D12.4, C20orf122, SWAM2, WAP2.
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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 MGSMASRGKT ETSKLKQNLE EQLDRLMQQL QDLEECREEL DTDEYEETKK ETLEQLSEFN DSLKKIMSGN MTLVDELSGM QLAIQAAISQ AFKTPEVIRL FAKKQPGQLR TRLAEMDRDL MVGKLERDLY TQQKVEILTA LRKLGEKLTA DDEAFLSANA GAILSQFEKV STDLGSGDKI LALASFEVEK TKK.
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 :
a-ActininDescription:
Actinin Alpha
Alpha-actinin-1, Alpha-actinin cytoskeletal isoform, Non-muscle alpha-actinin-1, F-actin cross-linking protein, ACTN1.
Product # :
PRO-518Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Ultra pure Alpha Actinin having a Molecular mass of 95,000 Dalton.
Source
Chicken Gizzard.
Formulation
The protein was lyophilized from a 1mg/ml solution containing 10mM Tris acetate buffer pH 7.6, 0.1mM EDTA, 2mM DTT, and 20mM NaCl.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
Citations
More Info
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Introduction
ACTN1 encodes a nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene. Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments.
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Synonyms
Alpha-actinin-1, Alpha-actinin cytoskeletal isoform, Non-muscle alpha-actinin-1, F-actin cross-linking protein, ACTN1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized a-Actinin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution a-Actinin 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 a-Actinin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Applications
Protein standard in 1D and 2D SDS gelelectrophoresis
Immunoassays
Immunization.
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 :
FGF8 Human, HEKDescription:
Fibroblast Growth Factor-8 Human Recombinant, HEK
FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.
Product # :
CYT-087Price :
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Shipped with Ice Packs
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Description
FGF-8 Human Recombinant is a single, glycosylated, polypeptide chain (23-215 a.a) containing a total of 204 amino acids and having a molecular mass of 23.7 kDa. FGF-8 is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK.
Formulation
The FGF-8 solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90% as obsereved by SDS-PAGE.
Biological Activity
The ED50 is ≤5 µg/ml, measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells in the presence of 10ug/ml of heparin.
Citations
More Info
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Introduction
FGF8 is part of the fibroblast growth factor family. FGF family members have wide mitogenic and cell survival activities, and participate in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF8 supports androgen and anchorage independent growth of mammary tumor cells. FGF8 over expression increases tumor growth and angiogensis. The adult expression of FGF-8 gene is restricted to testes and ovaries. FGF8 functions as an embryonic epithelial factor. FGF8 takes part in midbrain and limb development, organogenesis, embryo gastrulation and left-right axis determination.
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Synonyms
FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
DGSHMQVTVQ SSPNFTQHVR EQSLVTDQLS RRLIRTYQLY SRTSGKHVQV LANKRINAMA EDGDPFAKLI VETDTFGSRV RVRGAETGLY ICMNKKGKLI AKSNGKGKDC VFTEIVLENN YTALQNAKYE GWYMAFTRKG RPRKGSKTRQ HQREVHFMKR LPRGHHTTEQ SLRFEFLNYP PFTRSLRGSQ RTWAPEPRHH HHHH.
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Background
What is the molecular weight/Mw of FGF8 Protein?
FGF8 Protein has a total Mw of 23.7kDa.
What is the source or expression system of FGF8 Protein?
HEK.
What is the Purity of FGF8 Protein?
FGF8 Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF8 Protein?
The ED50 is ≤5 µg/ml, measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells in the presence of 10ug/ml of heparin.
What is the amino acid sequence of FGF8 Protein?
DGSHMQVTVQ SSPNFTQHVR EQSLVTDQLS RRLIRTYQLY SRTSGKHVQV LANKRINAMA EDGDPFAKLI VETDTFGSRV RVRGAETGLY ICMNKKGKLI AKSNGKGKDC VFTEIVLENN YTALQNAKYE GWYMAFTRKG RPRKGSKTRQ HQREVHFMKR LPRGHHTTEQ SLRFEFLNYP PFTRSLRGSQ RTWAPEPRHH HHHH.
What applications can FGF8 Protein be used in?
FGF8 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF8 Protein?
The endotoxin level is minimal, FGF8 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 :
GHRLDescription:
Ghrelin Human
Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.
Product # :
HOR-297Price :
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Shipping Method :
Shipped at Room temp
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Description
Ghrelin Human contains 28 amino acids and a total molecular mass of 3370.9 Dalton and a molecular formula of C149H249N47O42.The GHRL is purified by proprietary chromatographic techniques.
Formulation
GHRL was lyophilized without additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Citations
More Info
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Introduction
Obestatin is a hormone that is produced in the cells lining the stomach and small intestine of several mammals including humans; it drastically reduces appetite in mice and is expected to do the same in humans. Obestatin is a peptide hormone - a relatively small protein. It is encoded by the same gene that also encodes ghrelin, a peptide hormone that increases appetite. The protein produced by that gene breaks into two smaller peptides, ghrelin and obestatin. Ghrelin is an endogenous ligand for the growth hormone secretagogue receptor and is involved in regulating growth hormone release. Ghrelin is derived from a preprohormone called preproghrelin, which also generates a second peptide called obestatin. Ghrelin is an endogenous ligand for the orphan G protein-coupled receptor GPR39 and is involved in satiety and decreased food intake.
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Synonyms
Appetite-regulating hormone precursor, Growth hormone secretagogue, Growth hormone-releasing peptide, GHRP, Motilin-related peptide, M46 protein, Ghrelin, Obestatin, MTLRP.
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Physical Appearance
Sterile Filtered Yellowish lyophilized (freeze-dried) powder that may appear as a gel form.
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Stability
Store the lyophilized Ghrelin at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted GHRL can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Add deionized water to a working concentration approximately 0.5mg/1ml and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
Gly-Ser-Ser(n-octanoyl)-Phe-Leu-Ser-Pro-Glu-His-Gln-Arg-Val-Gln-Gln-Arg-Lys-Glu-Ser-Lys-Lys-Pro-Pro-Ala-Lys-Leu-Gln-Pro-Arg-OH.
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Background
What is the molecular weight/Mw of GHRL Protein?
GHRL Protein has a total Mw of 3.37kDa.
What is the Purity of GHRL Protein?
GHRL Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of GHRL Protein?
The biological functionality of GHRL Protein will be determined in the future.
What is the amino acid sequence of GHRL Protein?
Gly-Ser-Ser(n-octanoyl)-Phe-Leu-Ser-Pro-Glu-His-Gln-Arg-Val-Gln-Gln-Arg-Lys-Glu-Ser-Lys-Lys-Pro-Pro-Ala-Lys-Leu-Gln-Pro-Arg-OH.
What applications can GHRL Protein be used in?
GHRL Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GHRL Protein?
The endotoxin level is minimal, GHRL Protein was purified using conventional chromatography techniques.
Who supplies GHRL that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of GHRL?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
MUC1 HumanDescription:
Mucin-1 (CA15-3) Human
Product # :
PRO-2747Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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- Citations
Description
The Human Mucin-1 (CA15-3) is having a molecular mass of approximately 400kDa, and was purified from human carcinoma cell line.
Source
Human carcinoma cell line.
Formulation
MUC1 is supplied in a 0.05M sodium phosphate buffer, pH 7.5, 0.09% NaN3 and 0.15M NaCl.
Purity
Greater than 60%.
Citations
More Info
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Introduction
Human Mucin-1 (CA15-3), aka MUC1, is a glycoprotein with extensive O-linked glycosylation of its extracellular domain. This protein has alpha and beta subunits that form a heterodimeric complex. The N-terminal alpha subunit roles in cell-adhesion and the C-terminal beta subunit is involved in cell signaling. Mucins line the apical surface of epithelial cells in the stomach, lungs, intestines, eyes and other tissues. Mucins protect the body from infection by pathogen binding to oligosaccharides in the extracellular domain, preventing the pathogen from reaching the cell surface. Overexpression of CA15-3 is often associated with colon, breast, ovarian, lung and pancreatic cancers.
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Physical Appearance
Clear to opalescent colorless frozen solution.
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Stability
Human MUC1 although stable at 4°C for 1 week, should be stored at -20°C.
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Human Virus Test
Tissue sample tested and found negative for HIV-1 & 2 antibodies, HBsAg, and Hepatitis-C antibodies, Syphilis and HIV/HBV/HCV NAT.
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 :
CRYAA HumanDescription:
Crystallin Alpha A Human Recombinant
CRYA1, HSPB4, CRYAA, Crystallin Alpha A, Alpha-crystallin A chain, Heat shock protein beta-4.
Product # :
HSP-002Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
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- purity
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Description
Recombinant Human CRYAA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 173 amino acids and having a molecular mass of 19.9kDa.CRYAA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CRYAA protein contains 20mM Tris-HCl buffer (pH 7.5), 50mM NaCl and 1mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Alpha crystallins are composed of two gene products ; alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein(sHSP also known as the HSP20). They act as molecular chaperones and hold them in large soluble aggregates. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional function of a-crystallins are an autokinase activity and participation in the intracellular architecture. The expression of alpha-A is preferentially restricted to the lens cell.
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Synonyms
CRYA1, HSPB4, CRYAA, Crystallin Alpha A, Alpha-crystallin A chain, Heat shock protein beta-4.
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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
MDVTIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSGISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ DDFVEIHGKH NERQDDHGYI SREFHRRYRLPSNVDQSALS CSLSADGMLT FCGPKIQTGL DATHAERAIP VSREEKPTSA PSS.
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 :
KLK3 ProteinDescription:
Kallikrein-3 Recombinant Human
Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1.
Product # :
ENZ-1102Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
Kallikrein-3 Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 237 amino acids and having a molecular mass of 26.1kDa.KLK3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 150mM NaCl and 3% trehalose.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
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Introduction
Kallikrein-3 (KLK3) is a part of the kallikrein-related peptidase family. Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins take part in carcinogenesis and some may be prospective cancer and other disease biomarkers. Kallikrein-3 is 1 of the 15 kallikrein subfamily members located in a cluster on chromosome 19 and is a protease present in seminal plasma. KLK3 hydrolyzes semenogelin-1 consequently leading to the liquefaction of the seminal coagulum. KLK3 acts normally in the liquefaction of seminal coagulum, probably by hydrolysis of the high molecular mass seminal vesicle protein. Serum level of the KLK3 protein, called PSA in the clinical setting, is beneficial in the diagnosis and monitoring of prostatic carcinoma.
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Synonyms
Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized KLK3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Kallikrein-3 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 Kallikrein-3 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
IVGGWECEKH SQPWQVLVAS RGRAVCGGVL VHPQWVLTAA HCIRNKSVIL LGRHSLFHPE DTGQVFQVSH SFPHPLYDMS LLKNRFLRPG DDSSHDLMLL RLSEPAELTDA VKVMDLPTQE PALGTTCYAS GWGSIEPEEF LTPKKLQCVD LHVISNDVCA QVHPQKVTKF MLCAGRWTGG KSTCSGDSGG PLVCNGVLQG ITSWGSEPCA LPERPSLYTK VVHYRKWIKD TIVANP.
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.