Every item is shipped based on the best shipping method assessed for the temperature requirements of that specific item. Items are grouped and shipped together whenever
possible, and a separate shipping charge will be included for each shipping method required. Shipping charges listed below are from our US warehouses to the Contiguous US,
Alaska, Hawaii, Canada and Puerto Rico. Shipping charges for countries outside the US and Canada will be determined once order has been received
Please note: We can not ship to PO boxes
Express Blue Ice
Express Dry Ice
Animal Health Prescription Item
SHIPPING METHODS & CHARGES
Ships via FedEx Ground to Contiguous US, Alaska, Canada, Monday through Friday. This method is used for less temperature sensitive items such as lab ware and animal
health products, bulky and/or heavy items
Labware ships FedEx Ground free of charge to the contiguous US
Hemoglobin ζ Antibody (C-1B3) is a high quality monoclonal Hemoglobin zeta antibody (also designated Hemoglobin subunit zeta antibody, zeta chain of hemoglobin tetramer antibody, zeta globin antibody, ζ-globin antibody, haemoglobin zeta antibody, haemoglobin subunit zeta antibody, early embryo yolk sac specific hemoglobin subunit zeta antibody, or alpha-like hemoglobin antibody) suitable for the detection of the Hemoglobin zeta protein of human origin. Hemoglobin ζ Antibody (C-1B3) is available as the non-conjugated anti-Hemoglobin zeta antibody. Hemoglobin (Hgb) is coupled to four iron-binding, methene-linked tetrapyrrole rings (heme). The α (16p13.3; 5′-ζ-pseudoz-pseudo α2-pseudo α1-α2-α1-œ1-3′) and β (11p15.5) globin loci determine the basic hemoglobin structure. The globin portion of hemoglobin consists of two α chains and two β chains arranged in pairs forming a tetramer. Each of the four globin chains covalently associates with a heme group. The bonds between α and β chains are weaker than between similar globin chains, thereby forming a cleavage plane that is important for oxygen binding and release. High affinity for oxygen occurs upon relaxation of the α1-β2 cleavage plane. When the two α1-β2 interfaces are closely bound, hemoglobin has a low affinity for oxygen. Hb A, which contains two α chains plus two β chains, comprises 97% of total circulating hemoglobin. The remaining 3% of total circulating hemoglobin is comprised of Hb A-2, which consists of two α chains plus two δ chains, and fetal hemoglobin (Hb F), which consists of two α chains together with two γ chains.
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.